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Database: UniProt
Entry: E4PKN8_MARAH
LinkDB: E4PKN8_MARAH
Original site: E4PKN8_MARAH 
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
//
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