BIOW_AQUAE
ID BIOW_AQUAE Reviewed; 240 AA.
AC O67575;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=aq_1659;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07525.1; -; Genomic_DNA.
DR PIR; F70443; F70443.
DR RefSeq; NP_214141.1; NC_000918.1.
DR RefSeq; WP_010881078.1; NC_000918.1.
DR PDB; 5TV5; X-ray; 2.50 A; A/B=1-240.
DR PDB; 5TV6; X-ray; 2.46 A; A/B=1-240.
DR PDB; 5TV8; X-ray; 2.55 A; A/B=1-240.
DR PDB; 5TVA; X-ray; 2.25 A; A/B=1-240.
DR PDBsum; 5TV5; -.
DR PDBsum; 5TV6; -.
DR PDBsum; 5TV8; -.
DR PDBsum; 5TVA; -.
DR AlphaFoldDB; O67575; -.
DR SMR; O67575; -.
DR STRING; 224324.aq_1659; -.
DR DNASU; 1193291; -.
DR EnsemblBacteria; AAC07525; AAC07525; aq_1659.
DR KEGG; aae:aq_1659; -.
DR PATRIC; fig|224324.8.peg.1281; -.
DR eggNOG; COG1424; Bacteria.
DR HOGENOM; CLU_076858_0_0_0; -.
DR InParanoid; O67575; -.
DR OMA; LCWSDDP; -.
DR OrthoDB; 1268552at2; -.
DR BRENDA; 6.2.1.14; 396.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin biosynthesis; Ligase; Magnesium;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..240
FT /note="6-carboxyhexanoate--CoA ligase"
FT /id="PRO_0000191014"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5TV6"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:5TVA"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:5TVA"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5TVA"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5TV5"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:5TVA"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5TVA"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:5TVA"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5TVA"
SQ SEQUENCE 240 AA; 27399 MW; 107D7EC0E6C32570 CRC64;
MDLFSVRMRA QKNGKHVSGA ERIVKKEELE TAVKELLNRP KEFDFMNVKV EKVKDFEVVK
FNLKISTYSF KSPEEAREFA VKKLTQEGIK EEVAKKAVEI LSKGANPKGG NMRGAVLMDI
ETGERLEEDK ERGVRTIHFD WKDRKKVTEK LLKEGYTLRT VDALALTFKN LFCGVVAELC
WSDDPDYVTG YVSGKEIGYV RITPLKEKGD PLGGRVYFVS RKELSEIIEC LTQKVVLIEL
