ID Q49X77_STAS1 Unreviewed; 586 AA.
AC Q49X77;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Putative pyruvate flavodoxin ferredoxin oxidoreductase alpha subunit {ECO:0000313|EMBL:BAE18621.1};
GN OrderedLocusNames=SSP1476 {ECO:0000313|EMBL:BAE18621.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE18621.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE18621.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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DR EMBL; AP008934; BAE18621.1; -; Genomic_DNA.
DR RefSeq; WP_011303240.1; NZ_MTGA01000034.1.
DR AlphaFoldDB; Q49X77; -.
DR KEGG; ssp:SSP1476; -.
DR PATRIC; fig|342451.11.peg.1479; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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 Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:BAE18621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371}.
FT DOMAIN 14..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..452
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 476..550
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64702 MW; 90CDEEF20707CA23 CRC64;
MKSQVSWKVG GQQGEGIEST GEIFATAMNR KGYYLYGYRH FSSRIMGGHT NNKIRVSTTP
VHAISDDLDI LIAFDQETIE LNHHEMREDS VIIADSKAKP EKPDNCRAQL IDLPFTATAK
ELGTALMKNM VAIGATCAVM DLDISDFETL ITNMFTKKGD KVVELNIEAL NEGYRLMNEQ
LNNVDADFIL DKTDGKPHLY MIGNDAIGLG ALSAGSRFMA AYPITPASEI MEYMIENLPK
VGGTVVQTED EIAAANMAIG SNYAGVRAFT ASAGPGLSLM MEAIGLSGMT ETPFVVINTQ
RGGPSTGLPT KQEQSDLMQM IYGTHGDIPK IVVAPTDAED AFYLTMEAFN LAEQYQCPVI
VLSDLQLSLG KQTVEQLDYN KIEINRGDMI QSDIEREEND KTYFKRYALT ESGVSPRPIP
GVKGGIHHVT GVEHNEEGKT SEAADNRQQQ MDKRMRKTEN LLIQNPVEAD VQHETADILY
LGFISTKGAI QEGKSRLESQ NIKVNHIQIR QLHPFPSETI QKEVDKASKV VVVEHNYQGQ
LANILKMNVN LGDKLVNQTK YDGTPFLPHE IEANGLEIAK EIKELV
//