ID E4PKN8_MARAH Unreviewed; 1091 AA.
AC E4PKN8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Protein containing carbamoyl phosphate synthetase, large subunit, ATP-binding / carboxyl transferase / carbamoyl phosphate synthase, large subunit, N-terminal / biotin carboxylase, C-terminal / bio... {ECO:0000313|EMBL:ADP98514.1};
GN OrderedLocusNames=HP15_2750 {ECO:0000313|EMBL:ADP98514.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98514.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP98514.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) 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; CP001978; ADP98514.1; -; Genomic_DNA.
DR RefSeq; WP_014578015.1; NC_017506.1.
DR AlphaFoldDB; E4PKN8; -.
DR STRING; 225937.HP15_2750; -.
DR KEGG; mad:HP15_2750; -.
DR PATRIC; fig|225937.3.peg.2778; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1038; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_009218_0_0_6; -.
DR OMA; GTQGMRN; -.
DR Proteomes; UP000007077; 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 GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 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; 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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; 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}; Transferase {ECO:0000313|EMBL:ADP98514.1}.
FT DOMAIN 2..450
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 485..556
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 838..1075
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1091 AA; 116649 MW; F6FE500BA78EA1AB CRC64;
MTFRSVLIAN RGEIAIRIAR ACSELGLRSV AVFSEDDDAS LHTRMADEAV ALTGHGVKAY
LDGAQLIDVA KAHGCEAIHP GYGFLAENAG FARSCEQAGL IFIGPSPDVL EGFGDKSAAR
ALAERCEVPL IKGINRSVNL TEARAFLDEH GPLMIKAIAG GGGRGMRAVH AATELDQAFQ
RCQSEAQAAF GNGSLYVEQL IARARHIEIQ IVGDGTGAVS HLWERDCSLQ RRNQKLIEIA
PSPLLDASIR DAMIDSALKL AGAVNYRGLG TFEFLVDEDH PGHFYFMEAN PRIQVEHTIT
EEITGVDLVQ TQLQLFGGLS LTDLALESAP HVRGFAIQAR INSETLHADG HATAATGTLS
TYEPPSGPGL RVDGYGYAGY TISPSFDSLL AKLVAHGSDY PSTLRRLYRA LCEFRLTGVS
SNIGLLQNLV RHSGVETWAV TTRFVEDNLK HLIPEATKTA HPHLHFGNAS ASAVEESPGA
TAAPAGTIGI EAPSSGTVVS IDVTPGDSVA IGDPIAVLEA MKMEFVVTAT NSGIIHTVVA
EPGTMVNDGQ ALVYLEPADV EAGGIQNEET VDLEYIRADL AEVLERHNLL TDQRRPGAVA
KRRKTAQRTA RENVEDLLDP DSFNEYGALA LAAQRRRRSA DKLAEMSPAD GLITAIGTVN
APEFGPETGR CATMAYDYTV FAGTQGLTNH RKADRILALA EQWRIPLVLF AEGGGGRPSD
TDANGVSFLD CHTFVGMARL SGVVPTLGIV SGRCYAGNAA LLGCCDTIIA TRDANLGMAG
PAMIEGGGLG RFSPEQVGPV SVMGPNGVID VLVEDETEAV SVAKKYLSYF QGTLEDWQCD
DQRRLRHLIP ENRMRVYDIR QVIETLADQD SVLELRSQFA PGLITALVRI EGRPMGLIAN
NPAHLGGAVD ASAGDKAARF MQLCNAHGLP ILSLCDTPGF MVGPDAEKQA TIRHISRMFV
AAAKLNVPFF TVILRKAYGL GAQAMAAGSM LTPFFTAAWP SGEFGPMGWE GAVRLGFAKE
LAAQPDEESR QTMFDTLVAK AYEQGKALNV ASYLEIDAVI DPQETRAWLI RGLNSTSGIQ
SGEGGKFVDT W
//