ID A0A1Y2K6Z9_9PROT Unreviewed; 181 AA.
AC A0A1Y2K6Z9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=MAIT1_03280 {ECO:0000313|EMBL:OSM05128.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM05128.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM05128.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM05128.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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 -!- 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:OSM05128.1}.
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DR EMBL; LVJN01000018; OSM05128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K6Z9; -.
DR STRING; 1434232.MAIT1_03280; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000194003; Unassembled WGS sequence.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR028161; Met8-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR NCBIfam; TIGR01470; cysG_Nterm; 1.
DR PANTHER; PTHR35330; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR PANTHER; PTHR35330:SF1; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR Pfam; PF10414; CysG_dimeriser; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000194003}.
FT DOMAIN 116..171
FT /note="Sirohaem synthase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF10414"
SQ SEQUENCE 181 AA; 20657 MW; 308F7FC449FD98D6 CRC64;
MTLLALELEG ELLALAEEGA LAWRREPFTP EMLDDVWFVL CADDNPELHM RLSRVCAQRR
IFLNVVDRKT HCSAIWPALV DRHPVVAALT TGGASPALSS WLRRRLQQAI PEGVDALAQW
LSAWRARVAK QRSTFALRAR FWREAFEQDK IPELYLEGRI QEADALLKQR LEGSEDGRKP
T
//
