ID F0IYP6_ACIMA Unreviewed; 662 AA.
AC F0IYP6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:GAN73689.1};
DE SubName: Full=Methylcrotonoyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:BAJ80906.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:BAJ80906.1};
GN OrderedLocusNames=ACMV_15590 {ECO:0000313|EMBL:BAJ80906.1};
GN ORFNames=Apmu_0097_66 {ECO:0000313|EMBL:GAN73689.1};
OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ80906.1, ECO:0000313|Proteomes:UP000007100};
RN [1] {ECO:0000313|EMBL:BAJ80906.1, ECO:0000313|Proteomes:UP000007100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ80906.1}, and DSM 11245 / JCM 8867
RC / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA Hosoyama A., Yamada R., Fujita N.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAN73689.1, ECO:0000313|Proteomes:UP000032662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN73689.1,
RC ECO:0000313|Proteomes:UP000032662};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AP012035; BAJ80906.1; -; Genomic_DNA.
DR EMBL; BANA01000096; GAN73689.1; -; Genomic_DNA.
DR RefSeq; WP_011942299.1; NZ_BANA01000096.1.
DR AlphaFoldDB; F0IYP6; -.
DR KEGG; amv:ACMV_15590; -.
DR HOGENOM; CLU_000395_3_1_5; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000007100; Chromosome.
DR Proteomes; UP000032662; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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.
DR PROSITE; PS00189; LIPOYL; 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, ECO:0000313|EMBL:BAJ80906.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 583..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 70276 MW; CF68A2773EFEB5B1 CRC64;
MFGSVLIANR GEIACRVIRT ARRMGLRSIA VFSDADAGAA HVAMADAAVR IGPPAAAESY
LAIDRIIEAA RRTGAEAIHP GYGFLSENAD FAEACAAAGL VFVGPPAEAI RAMGSKSAAK
ALMEQAGVPL VPGYHGADQD PAALARAAAE IGYPVLIKAS AGGGGKGMRV VRAAADFAAE
LDRAKGEARA AFGDDRVLVE KYLTKPRHIE IQVFADTHGN VVSLHERDCS IQRRHQKIVE
EAPAPLIDEA MRAAMGKTAC DAARAIGYVG AGTVEFIAED GAFHFMEMNT RLQVEHPVTE
MITGIDLVEW QFRVAAGEAL PLKQEGIGRR GHAVEVRLYA EDPARDFAPS TGALARLRLP
AESRHLRIES GVRAGDEVSV HYDPMIAKLV TWDEDRDGAL RHMAQALAAC EIDGVQTNLD
LLRRIVTHPD FCAAALDTGF IARHEAALLP ARGAPPVAVL AAAAHRWLAT LPQSGDPSDP
WSPWATRAAW RLNGERFQDV VIEDGEATHH LRLHPRDERH FRLDHAGREV FVCVDAAGED
EVSVEIDGIV ARLGTSGQGG RIVVFADGAR HVLAVADPHR AAGEADGAAA RVTSVMPGKV
VELAVAAGSA VREGDLLAVI EAMKVQFRIT APRDGVIAAL HCAVGDLIED GAELMAFATD
TD
//
