ID A0A1I3BXC4_9RHOB Unreviewed; 1095 AA.
AC A0A1I3BXC4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Biotin-requiring enzyme {ECO:0000313|EMBL:SFH66954.1};
GN ORFNames=SAMN05216258_101416 {ECO:0000313|EMBL:SFH66954.1};
OS Albimonas pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFH66954.1, ECO:0000313|Proteomes:UP000199377};
RN [1] {ECO:0000313|EMBL:SFH66954.1, ECO:0000313|Proteomes:UP000199377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFH66954.1,
RC ECO:0000313|Proteomes:UP000199377};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOQH01000001; SFH66954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3BXC4; -.
DR STRING; 1114924.SAMN05216258_101416; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000199377; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; PS50989; COA_CT_CTER; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000199377}.
FT DOMAIN 2..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 481..558
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 838..1077
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1095 AA; 116305 MW; 1FF89BF5DB617040 CRC64;
MTIRRLLIAN RGEIAVRIAR TAAEMRIETV AVFPEDDAKT LHVRACDHAE PIPGRGARAY
LDAQALVAAA QRAGADAVHP GYGFLSESVA FARACEHAGL TWVGPTPASL ALFGDKVEAR
AHAARHDVPT IPGSSGPVDA AGAEAVFDQL PEGAALVIKA VAGGGGRGMR VVHAREEIAE
AHARCTSEAA AAFGDGAVYA ERFLPAARHI EVQVLGDGTG ECLHLLERDC TLQRRHQKVL
EIAPAPGLDA AAREALVSHA LKLARAGDYR SLGTFEFLAL PDASEVFFIE ANPRIQVEHT
VTEEILGLDL VRLQLEIASG RTLAELGLAQ KMVPQPSGYA IQARVNAERM DARGQARPSV
GKLTKWEPPF GPGVRIDTLA YSGWGNSPAY DSLIAKVIVH SRSPDFGDAL RKIDRALGEL
KAVGIETNAR WLRALARRPE VEGYAVTTRF IESVAGELAE AAAALPDPAA EEETAETAQA
AKAEALPEGA IPLAAPTIGT VTQVPEPGAR LRRGEVAALM ESMKMEHAVT SPVSGEVLKV
LAAAGDTLDE GAPILALMPD AEQDETEDAA AAVDLDHIRA DLQEVRDRLY AGMDESKPDK
VAKRHGRGQR TARENLASLA DPGSFQEYGG LVIAAQAARR SEDDLVKNTT GDGVVTGIGT
INAEKFGTEK GRCAFTIYDY MVLAGTQGQR HHRKLDRIFT MAGEYRMPMI VLAEGGGGRP
GETERRSVAG LDGPSFARFA ALSGKAPLVG VVSGRCFAGN AALLGCCDII IADESSNIGM
AGPAMIEGGG LGVYAPEDIG PIDVQSRNGV VDIRVKDEVE ACAAAKKYIS YFQGDEAEWT
APDQRLLRHA IPENRLRAHD VRHVIETMSD DGSVLELRRE FGLGIVTALV RIEGKPFGLI
ANDSRYLGGA IDAPAADKAA RFLQICDTFG LPVISLVDTP GFMVGPEAEK TALVRHVSRM
FVAAAGITVP IFAVVLRKGY GLGAMAMTGG GFHESLFTIS WPTGEFGGMG LEGAVHLGFR
KELEAKTDPK EKQALFDELL AKMYASGKAI QAAITAELDA VIDPVETRQW ILAGLRSVPA
ERLTGGKGRT YIDAW
//
