ID A0A1H3KUD5_9PSEU Unreviewed; 1081 AA.
AC A0A1H3KUD5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Biotin-requiring enzyme {ECO:0000313|EMBL:SDY55368.1};
GN ORFNames=SAMN05216215_102917 {ECO:0000313|EMBL:SDY55368.1};
OS Saccharopolyspora shandongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=418495 {ECO:0000313|EMBL:SDY55368.1, ECO:0000313|Proteomes:UP000199529};
RN [1] {ECO:0000313|EMBL:SDY55368.1, ECO:0000313|Proteomes:UP000199529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDY55368.1,
RC ECO:0000313|Proteomes:UP000199529};
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};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR EMBL; FNOK01000029; SDY55368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3KUD5; -.
DR STRING; 418495.SAMN05216215_102917; -.
DR OrthoDB; 9803706at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000199529; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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; 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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 6..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 467..544
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 561..830
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 824..1063
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1081 AA; 114709 MW; 14B027115E4C87B0 CRC64;
MGIGEPFGTL LVANRGEIAL RVFRAAAVLG VGTVGVHAAD DADSLHVARC DEAVPLPQNG
AAAYLDVAAI IEAARKTGAQ AIHPGYGFLS ENPALARACA DAGIAFVGPD PSALELFGDK
AKARALATEL EIPTLPGTAV ATLAGMERFL DTLEPDLSRG RGAAVIKAVA GGGGRGMRVV
RGRDELAEAF RACEAEALAA FGSGDLYIER LLTDARHIEV QVIGDGQAVA HLWDRDCSVQ
RRHQKLIEVA PAQGLDQRLR QDVLQAATRL VGAAAYRGVA TVEFLVSGQE FFFMEVNPRL
QVEHTVTEEV LGLDLVRSQL EIAAGASLAD LGLDQDRVPC PRGSAIQIRI NAETMTADGQ
VLPQSGVLDR FAMPAGRGIR VDTAGYPGYR TNPGFDSLLA KIVVHDAAGF TAARRLAVQA
LDELQITGVA TNLPLQQAIL RTDEFAAGRC ATSYVDNHRA ELLEAAPNAV PDAPLGATVA
PMSGSVVAVE VSLGDVVARG QVVMVLEAMK MQHVIRADSG GEVTQIRFRE GDVVDAGEPV
VIVSGNDGPG LADLADERID PDHIRPDLAR VLERKSLWAD ENRPEAVQKR HSRGMRTARE
NVTDLVDEGT FTEYGGFAIA AQRKRRELDD LLRNTPADGM ITGVGQVNGA QFGPERSTCA
VLAYDYTVLA GTQGYFNHRK TDRILEVARQ QQYPVVLFAE GGGGRPGDVD IPKGGGLITP
SFLALGELSG RVPTIGIAAG RCYAGNAALL GTCDVVIATR DANIGMGGPA MIEGGGLGVF
APEEIGPIDV QTANGVVDVA VEDEAEAVAV AKRYLSYFQG DVTDYSEPDQ RGLRHVVPEN
RKRAYDVHTA IDVLCDEGSV LELRPEFGRC TITALVRIAG RPMGLIANNP MVLGGAIDAD
GADKLARMLQ LCEVFGLPVV SLCDTPGFMV GPESEKTATV RHFGRMFVHG ARLTVPMATV
VLRKSYGLGA MAMAGGTMVK PALTVAWPSG EVGGMGLEGA VRLGFRRELE AIADPSQRRR
RYDELVAQMY ETGSAINTAM HLEIDDVVDP ADTRDLLLRA LPPVARTGWT NPRARAVIDA
W
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