ID K2JDT9_HELPX Unreviewed; 407 AA.
AC K2JDT9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate synthase subunit porA {ECO:0000313|EMBL:EKE81561.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:EKE81561.1};
GN Name=porA {ECO:0000313|EMBL:EKE81561.1};
GN ORFNames=OUE_0838 {ECO:0000313|EMBL:EKE81561.1};
OS Helicobacter pylori R030b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145111 {ECO:0000313|EMBL:EKE81561.1, ECO:0000313|Proteomes:UP000006761};
RN [1] {ECO:0000313|EMBL:EKE81561.1, ECO:0000313|Proteomes:UP000006761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R030b {ECO:0000313|EMBL:EKE81561.1,
RC ECO:0000313|Proteomes:UP000006761};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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:EKE81561.1}.
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DR EMBL; AMOR01000003; EKE81561.1; -; Genomic_DNA.
DR RefSeq; WP_001129862.1; NZ_AMOR01000003.1.
DR AlphaFoldDB; K2JDT9; -.
DR PATRIC; fig|1145111.4.peg.823; -.
DR Proteomes; UP000006761; Unassembled WGS sequence.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EKE81561.1};
KW Pyruvate {ECO:0000313|EMBL:EKE81561.1}.
FT DOMAIN 22..246
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 268..372
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 407 AA; 44751 MW; D19C6619D29DEF7C CRC64;
MAKSIELQEI EVWDGNTASS NALRQAQIDV IAAYPITPST PIVQNYGSFK DNGYVDGEFV
LVESEHAAMS ACVGAAAAGG RVSTATSSQG LALMVEVLYQ ASGMRLPIVL NLVNRALAAP
LNIHGDHSDM YLSRDSGWIS LCTCNPQEAY DFTLMAFRIA EHQKVRVPTI VNQDGFLCSH
TVQNVRPLSD AVAYQFVGEY QTKHSLLDFD KPVSYGAQAE EEWHYEHKAQ LHHAIMNASS
VIEEVFNDFA KLTGRQYQLT KTFQLEDAEI AIFALGTTYE SAIVAAKEMR KKGIKAGVAT
IHSLRPFPYE RLGQDLKNLK ALAILDKSSP AGAMGAMFNE VTSAVYQTQG TKHPVVSNYI
YGLGERDMTI AHLCEIFEEI NEDALKGTLT HPTQQFVGLR GPKMSFF
//
