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Database: UniProt
Entry: A0A0J1GJA8_9GAMM
LinkDB: A0A0J1GJA8_9GAMM
Original site: A0A0J1GJA8_9GAMM 
ID   A0A0J1GJA8_9GAMM        Unreviewed;       474 AA.
AC   A0A0J1GJA8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Siroheme synthase {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              Short=Urogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=2.1.1.107 {ECO:0000256|HAMAP-Rule:MF_01646};
DE     AltName: Full=SUMT {ECO:0000256|HAMAP-Rule:MF_01646};
DE     AltName: Full=Uroporphyrinogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              Short=UROM {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Precorrin-2 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=1.3.1.76 {ECO:0000256|HAMAP-Rule:MF_01646};
DE   Includes:
DE     RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000256|HAMAP-Rule:MF_01646};
DE              EC=4.99.1.4 {ECO:0000256|HAMAP-Rule:MF_01646};
GN   Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646};
GN   ORFNames=ABT58_16055 {ECO:0000313|EMBL:KLU99754.1};
OS   Photobacterium aphoticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99754.1, ECO:0000313|Proteomes:UP000036426};
RN   [1] {ECO:0000313|EMBL:KLU99754.1, ECO:0000313|Proteomes:UP000036426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99754.1,
RC   ECO:0000313|Proteomes:UP000036426};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent
CC       methylations of uroporphyrinogen III at position C-2 and C-7 to form
CC       precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring
CC       dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it
CC       catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
CC       {ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC         Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC         precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC         Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76;
CC         Evidence={ECO:0000256|ARBA:ARBA00001156, ECO:0000256|HAMAP-
CC         Rule:MF_01646};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025705, ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005010, ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC       methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC       dehydrogenase / sirohydrochlorin ferrochelatase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01646}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU99754.1}.
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DR   EMBL; LDOV01000028; KLU99754.1; -; Genomic_DNA.
DR   RefSeq; WP_047875454.1; NZ_LDOV01000028.1.
DR   AlphaFoldDB; A0A0J1GJA8; -.
DR   PATRIC; fig|754436.4.peg.3405; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000036426; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.8.210; Sirohaem synthase, dimerisation domain; 1.
DR   HAMAP; MF_01646; Siroheme_synth; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR028281; Sirohaem_synthase_central.
DR   InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR   InterPro; IPR006367; Sirohaem_synthase_N.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   NCBIfam; TIGR01470; cysG_Nterm; 1.
DR   PANTHER; PTHR45790:SF1; SIROHEME SYNTHASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF10414; CysG_dimeriser; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF14824; Sirohm_synth_M; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01646};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01646};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01646}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_01646}; Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01646}.
FT   DOMAIN          124..145
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          150..205
FT                   /note="Sirohaem synthase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
FT   DOMAIN          216..425
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   REGION          1..203
FT                   /note="Precorrin-2 dehydrogenase / sirohydrochlorin
FT                   ferrochelatase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   REGION          214..474
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   ACT_SITE        246
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646,
FT                   ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        268
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646,
FT                   ECO:0000256|PIRSR:PIRSR036426-1"
FT   BINDING         22..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         43..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         223
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         299..301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         304
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         329..330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   BINDING         410
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01646"
SQ   SEQUENCE   474 AA;  52153 MW;  CBF238F44B8CA03F CRC64;
     MDYLPIFADL KRRPCLVVGG NEIAWRKTRM LLKAGADVKV IAPELSAEFQ HAIAENQIDY
     LGETFQPEDL DGIFLAIAAT ERKALNALVY QSANQRQVLV NVVDDTQRCS FIVPSIVDRS
     PIIVAISSSG KAPVLARLLR EQLEALLPHH LGTMAEMAGR FRSRLAQKVT AFSARRRFWE
     QAFSGRFASQ VAAGDLAQAE QTLEDLSNGI EDRGEVALIG AGPGDPGLLT LRALQLMQQA
     DVVLYDYLVS DDVMDLVRRD AEWVCVGKKA GFHSVPQSET NRLIVQYAEQ GKRVVRLKGG
     DPFVFGRGGE ELEVLFDRQI PFEVVPGITA AAGATAYAGI PLTHRDYAQT AMFVTGHLKP
     DGKQLDWRTL ARGNQTLVIY MGLMNSRDIQ LQLIEHGRAP DTPIAIIERG TQRAQKVFKG
     QLDGLAELAQ QAESPSLIVI GEVVNLSEKL HWFGKQEQPL QSATRQPTAV VKLA
//
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