ID A0A372J540_9ACTN Unreviewed; 420 AA.
AC A0A372J540;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000313|EMBL:RFU22284.1};
DE EC=2.1.1.107 {ECO:0000313|EMBL:RFU22284.1};
GN Name=cobA {ECO:0000313|EMBL:RFU22284.1};
GN ORFNames=D0Z06_06370 {ECO:0000313|EMBL:RFU22284.1};
OS Geodermatophilus sp. LHW52908.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU22284.1, ECO:0000313|Proteomes:UP000262362};
RN [1] {ECO:0000313|EMBL:RFU22284.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52908 {ECO:0000313|EMBL:RFU22284.1};
RA Li L., Lin H.W.;
RT "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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; 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:RFU22284.1}.
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DR EMBL; QVQH01000004; RFU22284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372J540; -.
DR OrthoDB; 9815856at2; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000262362; 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 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; IPR012409; Sirohaem_synth.
DR InterPro; IPR006367; Sirohaem_synthase_N.
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; PF13241; NAD_binding_7; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 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:0000313|EMBL:RFU22284.1};
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:UP000262362};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RFU22284.1}.
FT DOMAIN 177..388
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ SEQUENCE 420 AA; 42831 MW; A005193C2F436E52 CRC64;
MNATSVDPGS GVVYPVGLRL LDRRVVVVGG GQVAHRRVAG LLEARARVTV VSPEVTPALE
ALVGPGAVTW VRRRYEAGDL AGAWYAVAAT DDPAVNAAVA EEAERSRVFC ARADDRAASS
VWTPAVGRQG DLVVGVHGGG DPQRAVGVRD AVLAGLTDGS IRDRAAREPE GGRPGGVVLV
GGGPGDPGLI TVRGQQAVAQ ADVVVADHLA PQGLLAALPP EVEVIDASKL PRGRFMAQEQ
INALLVEHAR AGRRVVRLKG GDPFVFGRGM EELEACVAAG VPVEVVPGVT SAIGVPALAG
IPVTHRGLTH EFVVVSGHVP PGHPASLVDW PALGRLRGTL VVLMGVDTAP AIAAALVEHG
RAPGTPVAVV ADGSTPGQRV VRTTLSGLAR TLADEGIRPP AVWVVGEVVG LTAGLPRPPG
//