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
//