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Database: UniProt
Entry: A0A0B4BGW5_9RHOB
LinkDB: A0A0B4BGW5_9RHOB
Original site: A0A0B4BGW5_9RHOB 
ID   A0A0B4BGW5_9RHOB        Unreviewed;       465 AA.
AC   A0A0B4BGW5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Siroheme synthase {ECO:0000313|EMBL:KIC47989.1};
GN   ORFNames=RA29_17415 {ECO:0000313|EMBL:KIC47989.1};
OS   Tateyamaria sp. ANG-S1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tateyamaria.
OX   NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC47989.1, ECO:0000313|Proteomes:UP000031171};
RN   [1] {ECO:0000313|Proteomes:UP000031171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(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}.
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:KIC47989.1}.
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DR   EMBL; JWLL01000009; KIC47989.1; -; Genomic_DNA.
DR   RefSeq; WP_039688373.1; NZ_JWLL01000009.1.
DR   AlphaFoldDB; A0A0B4BGW5; -.
DR   STRING; 1577905.RA29_17415; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000031171; 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   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:UP000031171};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          150..202
FT                   /note="Sirohaem synthase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
FT   DOMAIN          219..427
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   465 AA;  49157 MW;  4B4D9E358D17229F CRC64;
     MKTFPMFLTM TDRRVVILGG GEQATQKCRL MLKTEAEIEV FAPALDVELQ ALADNGRITH
     RTGPITAEAL RGAPLVFVGT GCPGIDAALH AVARDAGALV NVVDQPDLCD AITPAIVDRD
     PVVVAIGTEG TAPVLARQVK TALERMLDPR LGDLAALAGR LRDYAAQRLG PRQRRDLWRW
     VFNGPLRAQH AREGDAAVAR AIKDVIRTGS VPAAAPAPVA LVGAGPGSSD LITLRGVQRL
     QEADIIFYDR LVDPGVLELA RRDAERVFVG KEPGCHAWPQ DKINAVIVAA AKRGQRVVRL
     KCGDPGVFAR GAEEAEALQA ANLEYEIVPG VTAASGAAAA VGGFLTERGK SDTLVLTTGR
     CADGNGVPDW VTHLTQRSNV AVYMGVAAAP SISDSLARAG LLDQIDLTAV SKAQHADQKV
     MRCRAADMVE ELDRAGIESP AILFLSHRDV STSGTAEPVP HLVAV
//
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