ID C0ZY83_RHOE4 Unreviewed; 408 AA.
AC C0ZY83;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Siroheme synthase CysG {ECO:0000313|EMBL:BAH33318.1};
DE EC=1.3.1.76 {ECO:0000313|EMBL:BAH33318.1};
DE EC=2.1.1.107 {ECO:0000313|EMBL:BAH33318.1};
DE EC=4.99.1.4 {ECO:0000313|EMBL:BAH33318.1};
GN Name=cysG {ECO:0000313|EMBL:BAH33318.1};
GN OrderedLocusNames=RER_26100 {ECO:0000313|EMBL:BAH33318.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH33318.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH33318.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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}.
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DR EMBL; AP008957; BAH33318.1; -; Genomic_DNA.
DR RefSeq; WP_019748046.1; NC_012490.1.
DR AlphaFoldDB; C0ZY83; -.
DR KEGG; rer:RER_26100; -.
DR PATRIC; fig|234621.6.peg.3098; -.
DR eggNOG; COG0007; Bacteria.
DR eggNOG; COG1648; Bacteria.
DR HOGENOM; CLU_011276_1_0_11; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000002204; Chromosome.
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, ECO:0000313|EMBL:BAH33318.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:BAH33318.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAH33318.1};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAH33318.1}.
FT DOMAIN 169..380
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ SEQUENCE 408 AA; 42352 MW; B51D36EF2EFD9DF7 CRC64;
MSESTADETN YLVGLNLTDR RVVVFGGGTV AQRRLGLLVA SGARVHVISR AFTPAVEGMA
TAGQITVEER PYADGDLEGA WYAIASTDEP ETNAAIVAEA ERRHIFCVRA DNAKHGTAVT
PASAEYDGMS IGILAGGDHR RSAAVRTAVV EGLQSGVLAD TAEPAAAGVA LVGGGPGDPD
LITVRGRRLL ARADVVVADR LAPPELLAEL GPDVEVIDAA KIPYGRAMAQ EAINAALIDN
AKAGKFVVRL KGGDPYVFGR GYEELEACAA AGVPVTVVPG ITSAISVPSA AGIPVTHRGV
THEFVVVSGH VAPDHPDSLV DWSALAKLRG TIVLLMAVER IDQFARALVD GGRPSTTPVT
VIQEGTLRTQ RELRADLATV AQRVKDEEIK PPAIIVIGPV AGFSVDAG
//
