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Database: UniProt
Entry: A0A0H4WHB0_9BORD
LinkDB: A0A0H4WHB0_9BORD
Original site: A0A0H4WHB0_9BORD 
ID   A0A0H4WHB0_9BORD        Unreviewed;      1213 AA.
AC   A0A0H4WHB0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:AKQ54638.1};
GN   Name=accA1_1 {ECO:0000313|EMBL:AKQ54638.1};
GN   ORFNames=ACR54_01301 {ECO:0000313|EMBL:AKQ54638.1};
OS   Bordetella hinzii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ54638.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|EMBL:AKQ54638.1, ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|EMBL:AKQ54638.1,
RC   ECO:0000313|Proteomes:UP000036382};
RX   PubMed=26316634;
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT   Humans.";
RL   Genome Announc. 3:e00965-e00915(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA   Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP012076; AKQ54638.1; -; Genomic_DNA.
DR   RefSeq; WP_029579296.1; NZ_LT906461.1.
DR   AlphaFoldDB; A0A0H4WHB0; -.
DR   STRING; 103855.ACR54_01301; -.
DR   KEGG; bhz:ACR54_01301; -.
DR   PATRIC; fig|103855.15.peg.1290; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG1984; Bacteria.
DR   eggNOG; COG2049; Bacteria.
DR   eggNOG; COG4770; Bacteria.
DR   Proteomes; UP000036382; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR003778; CT_A_B.
DR   InterPro; IPR003833; CT_C_D.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR014084; Urea_COase.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   NCBIfam; TIGR02712; urea_carbox; 1.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF02626; CT_A_B; 1.
DR   Pfam; PF02682; CT_C_D; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SMART; SM00797; AHS2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT   DOMAIN          1..444
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1129..1204
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1213 AA;  130989 MW;  4407E47FEC28E9FC CRC64;
     MFDTVLIANR GEIALRAIRT LKRLGVRSVA VYSDADRDAA HVRQADVAIA LGGEKAADSY
     LRIDLLLEAA RRTGAQAVFP GYGFLSESAE FAAACEAAGL AFVGPTPGQI EEFGLKHRAR
     ELARAAGVPM TPGTGLLPNL GQALLEAERI GYPVMLKSTA GGGGIGLSRC ANEAELTAAY
     EGVQRLGEHF FRDGGVFIER YVDRARHVEV QIFGDGQGRV VALGERDCSV QRRNQKVIEE
     TPAPHLPEAT RAALLEAAVR LGVSVGYRSA GTVEFIYDER AGQFYFLEVN TRLQVEHPVT
     ECVTGLDLVE CMLRVAAGDG LDWEAMARPP EGAAIEVRLY AEDPLKQFQP SPGVLTEVSF
     PPGPRVDGWI STGTEVPAFY DPLLAKLIVH GRDRAQALQR LSEALGATRL HGIATNLDYL
     RQIVDDPAFR AGHVSTRFLE GFAYRPAMLE VLEPGTYTSV QDYPGREGYW DIGVPPSGPM
     DDYAFRLANR IVGNAPGAAG LEATLLGPSL RFHGDALIAL TGAPCAATLD GEPVAMWQPI
     TVKSGQVLAT GRVQNGCRLY LAVREGLDVP VYLGSRSTFA LGQFGGHAGR VLRMGDMLPL
     GRPELPASLA PHATLAPAAA PAALIPAYGQ HWEIGVLYGP HGAPDFFTPE AMDSFFAADW
     EVHYNSNRLG VRLIGPKPAW ARENGGEAGL HPSNIHDCEY AIGSINFTGD SPVILTRDGP
     SLGGFVCPAT IARAELWKVG QVKPGDRIRF KRISYEAAVA LEAAQDRAIA TLAPVPPEAV
     TVGTARAATV SETVVAELPA REGRPSVAYR QAGDGYLLLE YGENVLDLAL RMRVHLLMEA
     LAADPIAGVR ELSPGVRSLQ IRYDSREIRQ GVLIEKLLRI EAALADVATL RIPTRVVYLP
     MAFEDSATLG AVQRYQETVR PQAPWLPNNV DFIQRINGLA RREDVERIVF EASYLIMGLG
     DVYLGAPCAV PIDPRHRLLT SKYNPARTFT AEGTVGIGGV YMCIYGMDSP GGYQLVGRTL
     PIWNKFLKNP VFQDGKPWLL RFFDQVRFYP VSEAELDVLR ADFREGRASL RIEEEVFDFA
     AHQRFLDEEA ASIAAFQARQ KTAFDAEVAL WKHEDTVVRE ALPDPDEAAA LAEDETLVAA
     DMCGSVWKVP VAVGQSVAAG DTLVIIEAMK MELAVIAPAA GVVRAIRCTP GKQVNSGDAL
     VVLAEESVSA PVL
//
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