ID A0A254QSC8_9RHOB Unreviewed; 470 AA.
AC A0A254QSC8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Siroheme synthase {ECO:0000313|EMBL:OWU80628.1};
GN ORFNames=ATO1_09965 {ECO:0000313|EMBL:OWU80628.1};
OS Phaeobacter sp. 22II1-1F12B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU80628.1, ECO:0000313|Proteomes:UP000197279};
RN [1] {ECO:0000313|EMBL:OWU80628.1, ECO:0000313|Proteomes:UP000197279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU80628.1,
RC ECO:0000313|Proteomes:UP000197279};
RA Lai Q., Li G., Shao Z.;
RT "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000256|ARBA:ARBA00025705}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005010}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879}.
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:OWU80628.1}.
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DR EMBL; AQQP01000005; OWU80628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QSC8; -.
DR OrthoDB; 9815856at2; -.
DR UniPathway; UPA00262; UER00211.
DR Proteomes; UP000197279; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:InterPro.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
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 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; 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:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR Pfam; PF10414; CysG_dimeriser; 1.
DR Pfam; PF13241; NAD_binding_7; 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.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000197279};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..206
FT /note="Sirohaem synthase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF10414"
FT DOMAIN 219..428
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT ACT_SITE 271
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ SEQUENCE 470 AA; 50262 MW; 21DC26D8CC66BE99 CRC64;
MKTFPMFLRM NGRTVVIAGG GEQAAQKCRL ILKTEATIRL LAPALDPELA ALHRAGRVEW
NASPITEQSF GGAALAFICT ECAETDAALH GLARAAGVLV NVVDRPDLCE AITPSIVDRD
PVVVAIGTEG TAPVLARQIK TRLEETLEPR LGDLAALAGR LRDLAATRLS PRARRDLWAW
VFGGEVRRTH ARGLEAHAAR RIKQAIETGE IPTDCTAPVA LVGAGPGSSD LITLRGVKRL
QEADIIFYDR LIDPEILELA RRDVERVYVG KAPGCHSWPQ DRINSVLVSA ARQGKRVVRL
KCGDPGVFAR GAEEADALRE AGIDYEIVPG VTSASAAAAA LGGFLTERGR TDSLVLTTAR
RREGDEGADW LTHIRQGSNV AVYMGVQAAP EIQATLEGAG LADAVAVRIV SNAQRANQQI
VTCRADALAD TITRENVANP AIIFLTQDRP TTVAHRPLPM RTAPDLSVVA
//