ID A0A1B7K229_9GAMM Unreviewed; 1017 AA.
AC A0A1B7K229;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Lactate dehydrogenase family Fe-S protein {ECO:0000313|EMBL:OAT54199.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:OAT54199.1};
DE EC=1.1.-.- {ECO:0000313|EMBL:OAT54199.1};
DE EC=1.3.1.98 {ECO:0000313|EMBL:OAT54199.1};
GN ORFNames=M998_0531 {ECO:0000313|EMBL:OAT54199.1};
OS Providencia heimbachae ATCC 35613.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1354272 {ECO:0000313|EMBL:OAT54199.1, ECO:0000313|Proteomes:UP000078224};
RN [1] {ECO:0000313|EMBL:OAT54199.1, ECO:0000313|Proteomes:UP000078224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35613 {ECO:0000313|EMBL:OAT54199.1,
RC ECO:0000313|Proteomes:UP000078224};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OAT54199.1}.
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DR EMBL; LXEW01000011; OAT54199.1; -; Genomic_DNA.
DR RefSeq; WP_068907385.1; NZ_LXEW01000011.1.
DR AlphaFoldDB; A0A1B7K229; -.
DR GeneID; 79028341; -.
DR PATRIC; fig|1354272.4.peg.546; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000078224; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:OAT54199.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078224}.
FT DOMAIN 48..281
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1017 AA; 113572 MW; 4FE99D571EABA44E CRC64;
MIPRISEAPH LNKLVIEFIH ELQEQGFTGD NGTSYAERLS MATDNSIYQL LPQAIVFPRS
SADVQILTRV AGQKKYRTLS FTPRGGGTGT NGQSLTEGIV VDMSRYMNRI LEINPEQGWV
KVEAGVIKDQ LNQFLKPYGY FFSPELSTSN RATLGGMINT DASGQGSLVY GKTSDHVLGV
KAMVLGGECI DTRSMPVELA QTIASEDSVV GRIYKTVLER CLEQRPLIEE KFPKLNRFLT
GYDLRHVFND ALTEFDLTRI LTGSEGSLAF ITEATLDITP LPKARRLVNV KYDSFESALR
NAPFMVNAKA LSVETVDSKV LNLAREDIVW HSVKSLITDV PNKEMLGLNI VEFSGDDVVE
IDRLMDNLCQ QLDELMANNY AGIIGYQTCN DLDDITRIYN MRKKAVGLLG NSKGAAKPIP
FVEDTCVPPE HLADYIVEFR ALLDSHQLNY GMFGHVDAGV LHVRPALDMC DPQQEILMKQ
ISDEIVALTA KYGGLLWGEH GKGFRAQYSP EFFGEVLYGE LRNIKAAFDP DNRLNPGKIC
PPAGIDAPMK QVDDIKRGTF DRQIPIQMRQ EFRGAMDCNG NGLCFNFDVK SPMCPSMKIS
GQRIHSPKGR ATLVREWLRL LAEQGVTPEN IEKGIRDNKP SLRGLIDKTR NSWKAKQGDY
DFSHEVKASM AGCLACKACS TQCPIKIDVP SFRAKFLALY HGRYLRPIRD HIVANVEASA
PLLSKVPSVF NFFLRQPLVQ KLSERTIGMV DLPLFSEPTL KQELLGHSAT EVTLEQLEGM
SPSLRENYVL VVQDPFTSYY DAKVVADFIR LIEKLGYKPV LLPFSPNGKA QHIKGFLARF
AKTASKTADF LNRVAKLQLP MVGVDPALVL CYRDEYHEIL GEDQCKFTVM LAHEWLITLP
DPQKLNEISQ QPWYFFGHCT ESTALPNSGN QWSALFARYG QKLTNVSVGC CGMAGTYGHE
VVNIENSKGI YNLSWQPAMS ALPKERCLSS GYSCRSQVKR MENTIIKHPI QALLEIV
//
