ID D6Z278_DESAT Unreviewed; 636 AA.
AC D6Z278;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Biotin/lipoyl attachment domain-containing protein {ECO:0000313|EMBL:ADH85653.1};
GN OrderedLocusNames=DaAHT2_0950 {ECO:0000313|EMBL:ADH85653.1};
OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfobulbaceae; Desulfurivibrio.
OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH85653.1, ECO:0000313|Proteomes:UP000001508};
RN [1] {ECO:0000313|Proteomes:UP000001508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC {ECO:0000313|Proteomes:UP000001508};
RG US DOE Joint Genome Institute;
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA Woyke T.;
RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001940; ADH85653.1; -; Genomic_DNA.
DR RefSeq; WP_013163183.1; NC_014216.1.
DR AlphaFoldDB; D6Z278; -.
DR STRING; 589865.DaAHT2_0950; -.
DR KEGG; dak:DaAHT2_0950; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_419728_0_0_7; -.
DR InParanoid; D6Z278; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000001508; Chromosome.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Reference proteome {ECO:0000313|Proteomes:UP000001508}.
FT DOMAIN 22..285
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 559..634
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 636 AA; 70940 MW; 23915411273A5D59 CRC64;
MERIVHGMSP GEAIETLRKA DGYYVTNTAR DLSQSDYKNR ILLHTDLLAA PAREAAGYFS
LEITGGASIH VDMLRKQVDP FLKLQLLREK MPKTMFQTLC RGINLFGYRP YPQNVIRMVV
REYAKYVDVW RVFDFLNHVP NMVAVFEEVQ KAGKILEPAV CFSTGPEHTD EFYVKKVGEI
LDVTGQEIVL CIKNHGGLGT PKRIGDLVNA ILQKYPDLVI HYHGHNTDGN DVGRITAAVQ
AGARIVDASD HAFSGFYGPP SILTAVNTLT EYGYKAIGLN EEAVVDTSEA LRNERQYYEY
FESQFKGFDP TVQIHKLPGG AAGSSFEQAT KGGFLNKMPT ILHDELPKVQ KELGNYWSVT
PGSQILWTTA VANVQAGDRY STPSGDLKNL LLGKYGPFPF YQPADWIYEK VFGANWREIL
EKEGGMDEIA DMDIEQERRD LAEKLGYEPT EQQLVNYLQH PNDAVAFFKF EEKFGKVYAL
PPSIFLRRGG FKLGEVLKFR DHYGKEHVVE VGPMQHDEAG TAHVYLNVDH HERRYEFEPE
VSESSGGAAK EVQLSKKEIE ELAAAGDYRA PFGANVCEVS VKAGDEVKAG DQLLVLEAMK
MQTPIKSEID GKVEKISVKV GDAVKAGGPL LEVKSS
//
