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Database: UniProt
Entry: M1XST0_NATM8
LinkDB: M1XST0_NATM8
Original site: M1XST0_NATM8 
ID   M1XST0_NATM8            Unreviewed;       614 AA.
AC   M1XST0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Propionyl-CoA carboxylase biotin carboxylase component {ECO:0000313|EMBL:CCQ37440.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:CCQ37440.1};
GN   Name=pccA {ECO:0000313|EMBL:CCQ37440.1};
GN   OrderedLocusNames=Nmlp_3309 {ECO:0000313|EMBL:CCQ37440.1};
OS   Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS   8.8.11).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37440.1, ECO:0000313|Proteomes:UP000011867};
RN   [1] {ECO:0000313|EMBL:CCQ37440.1, ECO:0000313|Proteomes:UP000011867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC   {ECO:0000313|Proteomes:UP000011867};
RX   PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA   Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA   Gross K., Schuster S.C., Oesterhelt D.;
RT   "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT   of a previously haloalkaliphilic genus.";
RL   Genome Announc. 1:e0009513-e0009513(2013).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; HF582854; CCQ37440.1; -; Genomic_DNA.
DR   RefSeq; WP_015410183.1; NC_020388.1.
DR   AlphaFoldDB; M1XST0; -.
DR   STRING; 268739.Nmlp_3309; -.
DR   GeneID; 14651802; -.
DR   KEGG; nmo:Nmlp_3309; -.
DR   eggNOG; arCOG01591; Archaea.
DR   HOGENOM; CLU_000395_3_1_2; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 31083at2157; -.
DR   Proteomes; UP000011867; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 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; 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, ECO:0000313|EMBL:CCQ37440.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT   DOMAIN          1..459
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..329
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          538..614
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          464..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  65850 MW;  DD455A584F8F7ED7 CRC64;
     MFEKVLVANR GEIAVRVMRA CEDLGIDTVA VYSEADKHGG HVRYADEAYN VGPARAADSY
     LDHDAVIDAA RKADADAIHP GYGFLAENAT FAAAVEATEG VTWVGPSAES MEQAGEKTKA
     RTTMEAADVP IVPGTTDPVT DVSEVEEFGE EYGYPIAIKA EGGGGGRGMK IVHSPDEAAD
     QLDAAKREGE AYFDNDSVYL ERYLENPRHI EVQILADEHG NVRHLGERDC SLQRRHQKVI
     EEGPSPALSE ELREEIGNAA RRGADAADYY NAGTFEFLVE EEQRDDGELL GPDANFYFLE
     VNTRIQVEHC VTEELTGVDI VKWQLRVAAG EEIDFAQEDV ELDGHAIEFR INAENAADDF
     APATGGELGT YDPPGGIGVR VDDALRQGDD LVTDYDSMVA KLIVHAGDRE ECFARSERAL
     SEYDIEGIPT IIPFHRLMLT DDAFGAGTHT TKYLDEHLDP ERVEAAQERW GADAESGADD
     GGETVEREFT VEVNGKRFEV NLEESGEFAA LAGGSGGGAA AGTAERPSRG RGSDDDGGAD
     IDVDGAVVEA EMQGTILSVD VEVGDSVAAG DVLCVLEAMK MENDVIAETG GTVAEIAVDE
     GDSVDQGDPL VALE
//
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