ID B2RIN4_PORG3 Unreviewed; 535 AA.
AC B2RIN4;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|PIRNR:PIRNR006439};
DE Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE EC=1.2.7.8 {ECO:0000256|PIRNR:PIRNR006439};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|PIRNR:PIRNR006439};
GN OrderedLocusNames=PGN_0710 {ECO:0000313|EMBL:BAG33229.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG33229.1, ECO:0000313|Proteomes:UP000008842};
RN [1] {ECO:0000313|EMBL:BAG33229.1, ECO:0000313|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC 2561 {ECO:0000313|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:12645, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57271,
CC ChEBI:CHEBI:57287; EC=1.2.7.8;
CC Evidence={ECO:0000256|PIRNR:PIRNR006439};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR006439};
CC Note=Binds 2 [4Fe-4S] clusters. In this family the first cluster has a
CC non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
CC {ECO:0000256|PIRNR:PIRNR006439};
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DR EMBL; AP009380; BAG33229.1; -; Genomic_DNA.
DR RefSeq; WP_012457717.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RIN4; -.
DR GeneID; 29255933; -.
DR KEGG; pgn:PGN_0710; -.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_017727_0_0_10; -.
DR OrthoDB; 9804603at2; -.
DR BioCyc; PGIN431947:G1G2V-779-MONOMER; -.
DR Proteomes; UP000008842; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR017721; IorA.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR006439};
KW Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|PIRNR:PIRNR006439};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006439};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW Pyruvate {ECO:0000313|EMBL:BAG33229.1};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 15..176
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 378..510
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 535 AA; 58359 MW; A79EE306D897D0CA CRC64;
MQKQLLLGVE AIAQAALDAG ISGVYAYPGT PSTEITEHIQ NSRMAKERNV HREWAANEKT
AMESALGMSY AGKRALVCMK HVGMNVAADC FMNAAITGAN GGMVIVAADD PSMHSSQNEQ
DSRVYGQFAM IPVMEPSNQQ EAYDMTRLAF DLSERLGTPV MMRITTRLAH SRAGVVPTEP
IGENELHLPE DKRQYVLLPG IAKKRYRILL DKQTDFVRES ENSPYTEYID AADKSKGIVA
CGIAYNYLME AFKAQVPYPV LKVTQYPIPH KQMERLLNEC GDIVVMEEGY PVVEQLLKGF
PGLERIKGRL DGTLPRDGEL NPDHVAKAFN IPVVEGEPIP DLVAARPPAL CKGCSHRDVY
DALNEVLTEY PNGRVFSDIG CYTLGALPPY EAINSCVDMG ASITMAKGAA DAGLFPAVSV
IGDSTFTHSG ITGLLDAINE NSNITVIISD NESISMTGGQ HSSAYGKVEA ICRGIGVDPD
HIKELLPVPK NHDELCSIIR EEINYEGVSV IIPRRVCIQK HARDAKAAKR AKAKE
//
