ID A0A1H8NBL9_9RHOB Unreviewed; 650 AA.
AC A0A1H8NBL9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SEO26803.1};
GN ORFNames=SAMN04490248_10391 {ECO:0000313|EMBL:SEO26803.1};
OS Salinihabitans flavidus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salinihabitans.
OX NCBI_TaxID=569882 {ECO:0000313|EMBL:SEO26803.1, ECO:0000313|Proteomes:UP000198893};
RN [1] {ECO:0000313|EMBL:SEO26803.1, ECO:0000313|Proteomes:UP000198893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27842 {ECO:0000313|EMBL:SEO26803.1,
RC ECO:0000313|Proteomes:UP000198893};
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; FODS01000003; SEO26803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8NBL9; -.
DR STRING; 569882.SAMN04490248_10391; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000198893; 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:UP000198893}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 566..642
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 650 AA; 68640 MW; 5132F5FA1F2E0003 CRC64;
MFDKILIANR GEIACRVIET ARALGVRTVA VYSEADAGAR HVAMADEAVH IGGAAPADSY
LKGDVIIAAA RETGAQAIHP GYGFLSENPD FVEAVEKAGL TFIGPSAEAI RKMGLKDAAK
ALMEEAGVPV VPGYHGRNQD PEHLWGVADG IGYPVLIKAV AGGGGKGMRL VERAEDFLDA
LESAQSEARG AFGNADVLIE KYIQRPRHIE VQVFGDGTRA VHLFERDCSL QRRHQKVIEE
APAPGMTDEM RAAMGAAAVR AAEAIGYKGA GTVEFIVDSA GGLRPDGFWF MEMNTRLQVE
HPVTEAITGV DLVEWQLRVA SGETLPARQE DLSINGHAFE VRLYAEDVPK GFLPATGTLS
HLVFPGSARA DTGVRAGDTI SPFYDPMIAK IITHGPTRAV ALARMRAALD RTQVAGTVTN
LAFLGALCAH AGFVRGEVDT GLIARDLYEL VKEPVPGAQV KALAALAALG LEGETDPMTG
FTLWEALGRS AHLRHDGEEF TAVVRSRGPG DHLVEVDGIT VEALRRGAGW LLDGERGAPV
VRHGLHVTVF AHHGIGFEVI DPLARDAHAA DAGHIVIAPM PGMVKAVFAE AGQTVAKGDR
LAILEAMKME HSLLAARDGV VAEVLAGAGT QVEAGAALIR LEDDDAEAAA
//