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Database: UniProt
Entry: A0A1V3PIY0_9GAMM
LinkDB: A0A1V3PIY0_9GAMM
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ID   A0A1V3PIY0_9GAMM        Unreviewed;       478 AA.
AC   A0A1V3PIY0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000313|EMBL:OOG48361.1};
GN   ORFNames=B0E52_02605 {ECO:0000313|EMBL:OOG48361.1};
OS   Rhodanobacter sp. C06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1945854 {ECO:0000313|EMBL:OOG48361.1, ECO:0000313|Proteomes:UP000189228};
RN   [1] {ECO:0000313|EMBL:OOG48361.1, ECO:0000313|Proteomes:UP000189228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C06 {ECO:0000313|EMBL:OOG48361.1,
RC   ECO:0000313|Proteomes:UP000189228};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
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, ECO:0000256|RuleBase:RU003960}.
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:OOG48361.1}.
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DR   EMBL; MUNP01000028; OOG48361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3PIY0; -.
DR   STRING; 1945854.B0E52_02605; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000189228; 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; 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};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003960};
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:UP000189228};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          119..145
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          150..207
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   478 AA;  50301 MW;  4FFA800A7BF08240 CRC64;
     MKLYPLFADL HGLPVLVVGG GGVARRKAEA LLGAGAQVTV GAPRLDAELA AWAGAGTIRW
     QRGEFVPGWL DGMWLVIAAT DERGLNAAVA AAASERRLFA NVVDDAAHSR FHVPAVVDRS
     PLVVAVSTAG AAPALARRVR ETLERVLDHG LGALVALAQR QRARIVRRHE NLADRRAFYD
     WLHDGPVLPL LRAARGQEAE QVLLAALQGD GPPPRKGSVT LVGAGPGHPG LLTLQALRAL
     NEADVVLHDQ LVGDAILAMV RRDAERIDVG KRCGGRQVAQ EQIHRLMLAH AREGRRVVRL
     KGGDPFVFGR GGEEMAFLRR HGVACAVVPG VTAAVACAAF AGIPLTQRGQ AQSVCLLTAH
     GKAGSDMPDV QALGRPGQTL AIYMGVERAD ALTARLLAHG RATDTPVAIV ENGSLPQQRV
     IAGVLAELPR LVREHAVGSP ALLIVGEVAA CATSQAWFGE LVDARAGQPV AEPMAELA
//
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