ID E9SZJ0_RHOHA Unreviewed; 1195 AA.
AC E9SZJ0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=uca {ECO:0000313|EMBL:EGD24947.1};
GN ORFNames=HMPREF0724_11482 {ECO:0000313|EMBL:EGD24947.1};
OS Prescottella equi ATCC 33707.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Prescottella.
OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD24947.1, ECO:0000313|Proteomes:UP000004245};
RN [1] {ECO:0000313|EMBL:EGD24947.1, ECO:0000313|Proteomes:UP000004245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD24947.1,
RC ECO:0000313|Proteomes:UP000004245};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD24947.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADNW02000007; EGD24947.1; -; Genomic_DNA.
DR RefSeq; WP_005517995.1; NZ_CM001149.1.
DR AlphaFoldDB; E9SZJ0; -.
DR STRING; 43767.A6I91_06755; -.
DR HOGENOM; CLU_002162_0_1_11; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000004245; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGD24947.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000004245}.
FT DOMAIN 4..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1117..1195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 669..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 127046 MW; 7759C4CA81E2A424 CRC64;
MFPAFDTLLV ANRGEIACRI VRSARELGLK TVAVYSDADA CAAHVEMADA AVRLGPAPAA
ESYLRTDKVI EAALATGAGA IHPGYGFLSE NEQFAAAAEQ AGIEFVGPTP DQLRVFGNKH
TAREAARAVG VPLVPGSGLL ESVEEALAEA ERIGYPVMLK AVGGGGGIGM QACFTPEALR
AAYDTVQRMA AANFSSSGVF LERFVARARH IEVQVFGDGA GRTVSLGTRD CSLQRRNQKV
VEEAPASGLP DHVTEQLLRS SRDLASSVNY RSAGTVEFVF DVDRGEASFL EMNTRLQVEH
PVTEEVTGVD LVAWMLRLAG GDASMLDGLP DSGPAITGHA VEARVYAEDP GRDYRPSAGT
LTSVQFPAAA RVETWVDTGT EVSAHYDPML AKIVTRGDTR EEAVAKLGGA LAETRLYGVQ
TNLPQLRHIC AQPLTDHTTS ALADIPATGP RIDVLRAGTM TTVQDLPGRI GLWQVGIPPS
GPMDDLSFRL ANTAVGNPVD APGLECTLQG PRLEFSTPTV VCVTGADAPV TVDGLAAAMW
EPIEIAAGSV LDIGAPADTG LRTYLAVRGG LDVPLFHGSA STFTLGGFGG VTGSAVATGD
VLGIRPESDT STAPARVPDD VRPELTHTWH LAVTEGPQPS PSYFTDADMT QFYETTWITA
SHANRTGIRL DGPKPTWSRT DGGDAGLHPS NLHDNPYSVG ALNVSGDTPI LLGPDGPSLG
GFACPLTVTS AHRWKMGQIR PGDAVRFVPV PDADADSLRR SDAMRAKDVP AVRVARGDGG
VLGRTDAGDD RPEVVYLRGG DDNILVEYGP MALDLGLRMR VHALSEALAD LQVSGLIDVT
PGVRSLHLHF DPDVLPQYRL LGVLQELESR LPATHDLVVP SRTVRLPLSF DDPSIAEAMA
RYRSGVRDTA PWLPSNTEFI RRINGLGSVD DVRKAVFDAE YLVLGLGDVY LGAPLAVPLD
PRHRLVTTKY NPARTWTPSD AVGIGGKYLC VYGMESPGGY QLIGRTVPIW SGYRQRAPFE
SGKPWLFRFF DRIVWEPVTP EQLEQARSDS RAGRFDADVS EGTFALADHL RFLEEHAESI
AEFEERQGAA FEAEKRAWHA AGEFDRVDAG PAPEPATEEL DVPPGAVVVE APMVGNVWRV
ELAPGQQVSA GDPAVVLEAM KLEMPVPCPA AGTVLQVLAE PGAKVAPGTP LAVIG
//
