BIOW_HYDTT
ID BIOW_HYDTT Reviewed; 244 AA.
AC D3DK66;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00668};
DE EC=6.2.1.14 {ECO:0000255|HAMAP-Rule:MF_00668};
DE AltName: Full=Pimeloyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00668};
GN Name=bioW {ECO:0000255|HAMAP-Rule:MF_00668};
GN OrderedLocusNames=HTH_1774, Hydth_1756;
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter.
OX NCBI_TaxID=608538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=20348262; DOI=10.1128/jb.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=21677850; DOI=10.4056/sigs.1463589;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H.,
RA Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., Jeffries C.D.,
RA Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., Goker M., Wirth R.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Hydrogenobacter thermophilus type strain (TK-
RT 6).";
RL Stand. Genomic Sci. 4:131-143(2011).
CC -!- FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA
CC with concomitant hydrolysis of ATP to AMP. {ECO:0000255|HAMAP-
CC Rule:MF_00668}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:14781, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36165, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57360, ChEBI:CHEBI:456215; EC=6.2.1.14;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00668};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00668};
CC -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis;
CC pimeloyl-CoA from pimelate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00668}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00668}.
CC -!- SIMILARITY: Belongs to the BioW family. {ECO:0000255|HAMAP-
CC Rule:MF_00668}.
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DR EMBL; CP002221; ADO46137.1; -; Genomic_DNA.
DR EMBL; AP011112; BAI70218.1; -; Genomic_DNA.
DR RefSeq; WP_012964398.1; NC_017161.1.
DR AlphaFoldDB; D3DK66; -.
DR SMR; D3DK66; -.
DR STRING; 608538.HTH_1774; -.
DR EnsemblBacteria; BAI70218; BAI70218; HTH_1774.
DR KEGG; hte:Hydth_1756; -.
DR KEGG; hth:HTH_1774; -.
DR PATRIC; fig|608538.5.peg.1790; -.
DR eggNOG; COG1424; Bacteria.
DR HOGENOM; CLU_076858_0_0_0; -.
DR OMA; LCWSDDP; -.
DR OrthoDB; 1268552at2; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000002574; Chromosome.
DR GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00668; BioW; 1.
DR InterPro; IPR005499; BioW.
DR Pfam; PF03744; BioW; 1.
DR TIGRFAMs; TIGR01204; bioW; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin biosynthesis; Ligase; Magnesium; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..244
FT /note="6-carboxyhexanoate--CoA ligase"
FT /id="PRO_0000412086"
SQ SEQUENCE 244 AA; 28195 MW; 0A388B50333B441E CRC64;
MRSVRMRAEL DGMHVSGAER VIPHYELEKV VMELLKRPKR YDKIVITIER VENLETIPKS
LPIKSHDFAD VEQAHEFVIK KLKEIGIEES ITQKALKLLT EGPNPKGGNM RGAVLMDPVS
GERLEPDQER GIRTTRIDWR NRTAIKEALR ERGIKKFYLE RLIDALAIAT KNIHCGVIAE
ICWSDDPEYT TGYIASKEFG YIRIKPMKEE HTPTGGRVYF VKRESLQELI ECLERKVMLI
EQLL