SIRC_PRIMG
ID SIRC_PRIMG Reviewed; 202 AA.
AC P61818;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Precorrin-2 dehydrogenase;
DE EC=1.3.1.76;
GN Name=sirC;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX PubMed=12408752; DOI=10.1042/bj20021443;
RA Raux E., Leech H.K., Beck R., Schubert H.L., Santander P.J., Roessner C.A.,
RA Scott A.I., Martens J.H., Jahn D., Thermes C., Rambach A., Warren M.J.;
RT "Identification and functional analysis of enzymes required for precorrin-2
RT dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and
RT cobalamin in Bacillus megaterium.";
RL Biochem. J. 370:505-516(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ASN-98; SER-101; SER-102; ASP-105 AND SER-124, AND SUBUNIT.
RX PubMed=18588505; DOI=10.1042/bj20080785;
RA Schubert H.L., Rose R.S., Leech H.K., Brindley A.A., Hill C.P., Rigby S.E.,
RA Warren M.J.;
RT "Structure and function of SirC from Bacillus megaterium: a metal-binding
RT precorrin-2 dehydrogenase.";
RL Biochem. J. 415:257-263(2008).
CC -!- FUNCTION: Catalyzes the dehydrogenation of precorrin-2 to form
CC sirohydrochlorin which is used as a precursor in both siroheme
CC biosynthesis and in the anaerobic branch of adenosylcobalamin
CC biosynthesis. It is unable to oxidize precorrin-3.
CC {ECO:0000269|PubMed:12408752, ECO:0000269|PubMed:18588505}.
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:0000269|PubMed:12408752, ECO:0000269|PubMed:18588505};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC sirohydrochlorin from precorrin-2: step 1/1.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12408752,
CC ECO:0000269|PubMed:18588505}.
CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin
CC ferrochelatase family. {ECO:0000305}.
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DR EMBL; AJ509159; CAD48923.1; -; Genomic_DNA.
DR PDB; 3DFZ; X-ray; 2.30 A; A/B=1-202.
DR PDBsum; 3DFZ; -.
DR AlphaFoldDB; P61818; -.
DR SMR; P61818; -.
DR BioCyc; MetaCyc:MON-18855; -.
DR BRENDA; 1.3.1.76; 656.
DR UniPathway; UPA00148; UER00222.
DR UniPathway; UPA00262; UER00222.
DR EvolutionaryTrace; P61818; -.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.8.610; -; 1.
DR InterPro; IPR028161; Met8.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042518; SirC_C.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR PANTHER; PTHR35330; PTHR35330; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01470; cysG_Nterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; NAD; Oxidoreductase;
KW Porphyrin biosynthesis.
FT CHAIN 1..202
FT /note="Precorrin-2 dehydrogenase"
FT /id="PRO_0000097773"
FT BINDING 20..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 98
FT /note="N->A: 4-fold decrease in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT MUTAGEN 101
FT /note="S->A: 1.4-fold increase in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT MUTAGEN 101
FT /note="S->D: 2.8-fold increase in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT MUTAGEN 102
FT /note="S->A: 2.3-fold increase in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT MUTAGEN 105
FT /note="D->A: 3.2-fold increase in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT MUTAGEN 124
FT /note="S->A: 3-fold decrease in the dehydrogenase
FT activity."
FT /evidence="ECO:0000269|PubMed:18588505"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3DFZ"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:3DFZ"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:3DFZ"
SQ SEQUENCE 202 AA; 22970 MW; 7AA89B591622DEAD CRC64;
MYTVMLDLKG RSVLVVGGGT IATRRIKGFL QEGAAITVVA PTVSAEINEW EAKGQLRVKR
KKVGEEDLLN VFFIVVATND QAVNKFVKQH IKNDQLVNMA SSFSDGNIQI PAQFSRGRLS
LAISTDGASP LLTKRIKEDL SSNYDESYTQ YTQFLYECRV LIHRLNVSKS RKHELLTEII
DDQYRLSLVK QREFLQQIEK YK
