ID H3SG32_9BACL Unreviewed; 768 AA.
AC H3SG32;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:EHQ61995.1};
GN ORFNames=PDENDC454_12435 {ECO:0000313|EMBL:EHQ61995.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61995.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61995.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61995.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ61995.1}.
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DR EMBL; AHKH01000027; EHQ61995.1; -; Genomic_DNA.
DR AlphaFoldDB; H3SG32; -.
DR STRING; 1131935.PDENDC454_12435; -.
DR PATRIC; fig|1131935.3.peg.2563; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; -; 3.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
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 Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:EHQ61995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 30..256
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 279..383
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT DOMAIN 552..656
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 768 AA; 84982 MW; 57C4F1920FF27CEC CRC64;
MAIEYDKEAM PSRVEQRMVY ESGNEMAAYA AHQINYHIMG YYPISPSTEV AQFLDLMKAS
GKHDIKLIPA DGEHGSAGIC YGASTAGGRV FNATSANGYL YMLEQMPVQS GTRFPMVLNL
VCRSVSGPLN IHGDHSDLYF ALNTGWPILL CRDPQAVYDM NMMAIKLAED PEVRLPVMVA
FDGYFTSHQK RRVQTFARRE DVQRFIGEQP VRGFADTLDR NNPITVGPYM NEPDYINNCY
QQSMAMYKAG EVFDRIRREY AELTGRDYPV LDLYRMEDAE VAVFLLNSAA EIIKDVVDQL
REQGIKAGAV SPNMIRPFPA KEIAAALAGV KAVTVGDRAD SYGGHGGNMV NEVKAALFTH
GNRDTLVISR IYGLGGKDFY AEDGHAMFRC ALEAAAAGAV AQPFDYIGHT PGDPAAAPKR
VLEPMKYEEL NTGLITVKQV EETGKLNVRI PPLRQLTKKP KRIAPGHGAC PGCGIFSGLE
LFFKGIEGDI VALFHTGCAM VVTTGYPYSS HKATYIHNLF QNGAATLSGV VEMFWERKRR
GELDALNLPD DFTFVMITGD GGMDIGMGPA IGAALRNHKM IILEYDNEGY MNTGAQLSYS
TPIGHRTSTS NVGKAQTGKM FHHKDTAQIM AATHIPYVFT GSEAFPQDLL KKAAKAQWYA
RNEGLVYGKI LITCPLNWLS EDRAGTQIVQ AAVDSCFFPL YEVERGVTTI TYDPEEKNKK
IPLLDWLTMM GKTKHLAKPE NAELLGVFER EVERRWSVLR AKHAHPDL
//
