ID K6ZZV4_9ALTE Unreviewed; 681 AA.
AC K6ZZV4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:AGH46135.1};
GN Name=mccA {ECO:0000313|EMBL:AGH46135.1};
GN ORFNames=C427_4030 {ECO:0000313|EMBL:AGH46135.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH46135.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH46135.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH46135.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP003837; AGH46135.1; -; Genomic_DNA.
DR RefSeq; WP_007634412.1; NZ_BAES01000009.1.
DR AlphaFoldDB; K6ZZV4; -.
DR STRING; 1129794.C427_4030; -.
DR KEGG; gps:C427_4030; -.
DR PATRIC; fig|1129794.4.peg.4016; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000011864; Chromosome.
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; 3.30.700.40; -; 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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000011864}.
FT DOMAIN 1..447
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 588..669
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 681 AA; 74716 MW; 6BE852E39233B0F7 CRC64;
MFTKLLIANR GEISCRIIKT AKRMGILTVA LYSDADQHAL HVEMADEAVH VGPSPSKDSY
LQAEKIIQIA LKVGADAIHP GYGFLSENAT FANLCEQNNI IFIGPPVSAI EAMGSKSAAK
NIMELAKVPL VPGYHGNDQS VDGLKSHADK MGYPVLLKAA AGGGGKGMRQ VWKSSEFNDA
LAAAKREAMS SFNDDLMLVE KYLTEPRHVE IQVFCDNFGD GVYLFERDCS VQRRHQKIIE
EAPAFGMTPA LRKQMGETAL KAAKAINYAG AGTVEFLLDS DGQFYFMEMN TRLQVEHPVT
EMITGQDLVE WQLRVANNEP LPLAQDALKI NGHAFEARIY AEDPSNDFLP ATGRLSLLQP
PIESRHVRVD TGVVQGDEVS VFYDPMIAKL IVWDENRDKA LARLTKALTE YHIDGVVTNI
EFLYNLASSA PFKAEQIDTG FIEKNHDLLL LNDKQDIKDL LPIAVLYLML SSQQNSASDV
QDQYSPWSLS NAWRANEQYL QNLELMVADK TFSVQVSQSG AVSQLKAGSQ TVFHINVDQQ
YYQCAGVIEK NQLISTVNGH KTIANVNAHQ DGHSVFCNGK VIRFKSLQAD IGATQDNNAD
AGFIAPMNGT VVAILVEPGE QVELGQTLMV MEAMKMEHSL KAPAAGSVSE FYFKAGELVD
GGTELLAFQA VQPNKIKNES A
//
