ID A5N1K9_CLOK5 Unreviewed; 393 AA.
AC A5N1K9;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=PorA {ECO:0000313|EMBL:EDK35005.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:EDK35005.1};
GN Name=porA {ECO:0000313|EMBL:EDK35005.1};
GN OrderedLocusNames=CKL_2997 {ECO:0000313|EMBL:EDK35005.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK35005.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK35005.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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DR EMBL; CP000673; EDK35005.1; -; Genomic_DNA.
DR RefSeq; WP_012103340.1; NC_009706.1.
DR AlphaFoldDB; A5N1K9; -.
DR STRING; 431943.CKL_2997; -.
DR KEGG; ckl:CKL_2997; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_002569_5_0_9; -.
DR Proteomes; UP000002411; Chromosome.
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:EDK35005.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT DOMAIN 16..240
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 262..366
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 393 AA; 43240 MW; 8E24A4D01C6B12A7 CRC64;
MSIKERLSGN EAIAIAIKQI EPDVMPAFPI TPSTEIPQYF TKYVADGKVR TEFIPVESEH
SSMGAAIGAQ AAGARTVTAT SSCGLALMWE LLYVAASSRL PITMAVVNRA LSGPININAD
HSDTMGARDS GWIQIYSENN QEAYDNFIQA VRIGAYKDVQ LPVMVCQDGF ITSHAVENIE
LIEDEKVKEF VGEYNPEHYL MNPNETMAVG PYDISAYYME HKRLQAQAMI NAEKVILEVA
EEFAEMTGRK YGFFEEYELE DAEYAIVVIN STAGTAKAAV NKLRQAGKKA GLLKIRVFRP
FPAKKIAEAL KNTKAIAVMD RSEGFSACGG PVFAEVRSAM FDVENVPKII NYVYGLGGRD
IAVNDIEKVY NDLSEIAESG TCGETYRFLG VRE
//
