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Entry: I2QML1_9BRAD
LinkDB: I2QML1_9BRAD
Original site: I2QML1_9BRAD 
ID   I2QML1_9BRAD            Unreviewed;       478 AA.
AC   I2QML1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Uroporphyrin-III C-methyltransferase {ECO:0000313|EMBL:EIG61017.1};
GN   ORFNames=Bra1253DRAFT_05786 {ECO:0000313|EMBL:EIG61017.1};
OS   Bradyrhizobium sp. WSM1253.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG61017.1, ECO:0000313|Proteomes:UP000005125};
RN   [1] {ECO:0000313|EMBL:EIG61017.1, ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|EMBL:EIG61017.1,
RC   ECO:0000313|Proteomes:UP000005125};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX   PubMed=26629308;
RA   Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA   Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA   Ivanova N., Kyrpides N., Reeve W.;
RT   "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT   Ornithopus compressus from the Greek Island of Sifnos.";
RL   Stand. Genomic Sci. 10:113-113(2015).
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, ECO:0000256|RuleBase:RU003960}.
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DR   EMBL; JH600073; EIG61017.1; -; Genomic_DNA.
DR   RefSeq; WP_007599840.1; NZ_JH600073.1.
DR   AlphaFoldDB; I2QML1; -.
DR   eggNOG; COG0007; Bacteria.
DR   eggNOG; COG1648; Bacteria.
DR   HOGENOM; CLU_011276_2_1_5; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000005125; 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.
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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          150..204
FT                   /note="Sirohaem synthase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
FT   DOMAIN          222..431
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   478 AA;  50345 MW;  CAACE4E8A1F3730C CRC64;
     MRFLPVFLDL KAGPVVLIGA GELLRAKLRV LAAAGARIRV HAIDGNQDLG LSSEDAARIN
     IAAADPLTAD LSGIIAVVCA GAGDVGVAMS ARAKALGLPV NVMDDLAHSS FIFPAIVDRG
     DVVVAVGTGG TSPVVARRVR EKIEALLPAR IGELAEFIGG FRKSINERIA EFPLRRRFWE
     RIIDGPIGAA VLAGRKSEAD AALKAISDPS AFARADKPEG SVALVGAGPG DPDLLTIKAL
     RALQDADIVF HDELVSPEIL DRIRRDTTRV PVGRRVGKPG IGQDAINKRM IEAAQSGQRV
     VRLKGGDPFV FGRGGEEVEA LRAAGVAYSI IPGITAGLGG AADFEVPLTY RHEATRITFL
     TAHKARDAEV VDWSTLTDTR MTVVVYMGMT AAPAIRAGLL AAGRSPETPV GVFARVTRPD
     AQGAIGTLRD LPELVRRTHG GPAILIIGDV VRHAGSLRRE TAEKTPKQII SDLLDAAE
//
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