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Database: UniProt
Entry: C3KR81_SINFN
LinkDB: C3KR81_SINFN
Original site: C3KR81_SINFN 
ID   C3KR81_SINFN            Unreviewed;       389 AA.
AC   C3KR81;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE            EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN   OrderedLocusNames=NGR_b11360 {ECO:0000313|EMBL:ACP22589.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP22589.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004;
RA   Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA   Liesegang H., Broughton W.J.;
RT   "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT   NGR234.";
RL   J. Bacteriol. 186:535-542(2004).
RN   [2] {ECO:0000313|EMBL:ACP22589.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
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DR   EMBL; CP000874; ACP22589.1; -; Genomic_DNA.
DR   RefSeq; WP_015887234.1; NC_012586.1.
DR   RefSeq; YP_002823342.1; NC_012586.1.
DR   AlphaFoldDB; C3KR81; -.
DR   KEGG; rhi:NGR_b11360; -.
DR   PATRIC; fig|394.7.peg.1539; -.
DR   HOGENOM; CLU_011276_2_1_5; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000001054; Plasmid sym pNGR234b.
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:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
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; IPR028161; Met8-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   InterPro; IPR028281; Sirohaem_synthase_central.
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   Pfam; PF14824; Sirohm_synth_M; 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.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:ACP22589.1};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN          152..172
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          179..233
FT                   /note="Sirohaem synthase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
FT   DOMAIN          243..354
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   389 AA;  41904 MW;  55281F1FC782D8F8 CRC64;
     MHALPPLPND RASKPQRVAA LATLPLFWSL KGKRAVVAGG SDGAAWKAEL LAACGAEVHI
     YASHADLGDG FLDLIARGAA DEDGSFVHHD ESWHDGIFGD AALAIADCDD DRGAEAFFKA
     ARLAGVPVNV IDKPQFCQFQ FGSIVNRSPV VVAISTDGAA PILAQAIRRR IETLLPPAIK
     RWAGIAQAIR ERVNGRLQPG VQRRAFWERF VDRAFIDTPE EGVEARLMVE MDRLATPRPP
     VGRVTIVGAG PGDAELLTLK SVRALQAADV ILYDERISND VLELARREAK RILVSQPSRD
     AGIQDGSASV NVLARAGKRV VRLQAGDPVT NADSQQEAAW LGKLGIPVEI VPGVADRRRG
     AWENDDAKTI IDAGMVEQAH EQRLRVAGH
//
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