ID N4TAM5_HELPX Unreviewed; 407 AA.
AC N4TAM5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate synthase subunit porA {ECO:0000313|EMBL:ENH60273.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:ENH60273.1};
GN Name=porA {ECO:0000313|EMBL:ENH60273.1};
GN ORFNames=HPHPA11_1434 {ECO:0000313|EMBL:ENH60273.1};
OS Helicobacter pylori Hp A-11.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992035 {ECO:0000313|EMBL:ENH60273.1, ECO:0000313|Proteomes:UP000012243};
RN [1] {ECO:0000313|EMBL:ENH60273.1, ECO:0000313|Proteomes:UP000012243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp A-11 {ECO:0000313|EMBL:ENH60273.1,
RC ECO:0000313|Proteomes:UP000012243};
RA Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT "Comparative Sequence Analysis of H. pylori Isolates.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:ENH60273.1}.
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DR EMBL; AOTW01000001; ENH60273.1; -; Genomic_DNA.
DR RefSeq; WP_003016686.1; NZ_AOTW01000001.1.
DR AlphaFoldDB; N4TAM5; -.
DR PATRIC; fig|992035.3.peg.1396; -.
DR Proteomes; UP000012243; 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:ENH60273.1};
KW Pyruvate {ECO:0000313|EMBL:ENH60273.1}.
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; 44744 MW; AAE3AE18EB54D1AE CRC64;
MAKSIELQEI EVWDGNTASS NALRQAQIDV IAAYPITPST PIVQNYGSFK DNGYVDGEFV
LVESEHAAMS ACVGAAAAGG RVSTATSSQG LALMVEVLYQ ASGMRLPIVL NLVNRALAAP
LNIHGDHSDM YLSRDSGWIS LCTCNPQEAY DFTLMAFRIA EHQKVRVPTI VNQDGFLCSH
TVQNVRPLSD AVAYQFVGEY QTKHSLLDFD KPVSYGAQAE EEWHYEHKAQ LHHAIMSASS
VIEEVFNDFA KLTGRQYHLT KTFQLEDAEI AIFALGTTYE SAIVAAKEMR KKGIKAGVAT
IHSLRPFPYE RLGQDLKNLK ALAILDKSSP AGAMGAMFNE VTSTVYQTQG TKHPVVSNYI
YGLGERDMTI AHLCEIFEEI NEDALKGTLT HPTQQFVGLH GPKMSFF
//
