ID A0A074MB05_9SPHN Unreviewed; 621 AA.
AC A0A074MB05;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:KEO89950.1};
GN ORFNames=EH32_02885 {ECO:0000313|EMBL:KEO89950.1};
OS Erythrobacter litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO89950.1, ECO:0000313|Proteomes:UP000027866};
RN [1] {ECO:0000313|EMBL:KEO89950.1, ECO:0000313|Proteomes:UP000027866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO89950.1,
RC ECO:0000313|Proteomes:UP000027866};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL Submitted (APR-2014) 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:KEO89950.1}.
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DR EMBL; JMIX01000013; KEO89950.1; -; Genomic_DNA.
DR RefSeq; WP_034906424.1; NZ_JMIX01000013.1.
DR AlphaFoldDB; A0A074MB05; -.
DR KEGG; elq:Ga0102493_111659; -.
DR PATRIC; fig|39960.10.peg.741; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000027866; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR006594; LisH.
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; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50896; LISH; 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:UP000027866}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 542..618
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 621 AA; 66161 MW; 4795C852286AF97A CRC64;
MITKLLIANR GEIACRIIRT ARAMGVATVA VYSDADAKAL HVRSADEAVH IGPSPAAESY
LVGDKIIAAA KETGAEAVHP GYGFLSENAA FAQAVIDAGL IWVGPKPSSI EAMGLKDAAK
KLMREAGVPV TPGYEGEDQS VERLSKEAEA IGYPVLIKAV AGGGGKGMRK VDAPADFAAA
LESCRREAKA SFGNDEVLLE KWITSPRHIE VQVFGDAHGN VVHMFERDCS LQRRHQKVIE
EAPAPGMDES TREAICAAAV RAAKAVDYEG AGTIEFIADA SEGLRADRIF FMEMNTRLQV
EHPVTEEITG VDLVEWQLRV ASGEPLPLAQ DELSINGHAI EARLYAEDPA KGFLPSTGRL
EMFSIDDGYT RIETGVEQDD EISPFYDPMI AKLVVHGEDR EAAIWRLEDC IEELLVYPVK
TNAPFLLRAL TSDEFESAAL DTGLIARNPE WSEAVELSQA ALDQAAIPFL ARNAGQRGPA
LTGYRLNAAP QMEVAMMLGD AVAKGDASRP FDGVLQFDDG ETVWVNLLGE TFALAPFASR
GSGAASAADG AIIAPMPGKV IALDVAEGEA VTAGQRLMVL EAMKMEHALT APFDGTVTAL
EASVGGQVQV EAVLCVVEPE A
//
