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
//