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Database: UniProt
Entry: A9B0Y8_HERA2
LinkDB: A9B0Y8_HERA2
Original site: A9B0Y8_HERA2 
ID   A9B0Y8_HERA2            Unreviewed;       653 AA.
AC   A9B0Y8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ABX05266.1};
GN   OrderedLocusNames=Haur_2628 {ECO:0000313|EMBL:ABX05266.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX05266.1, ECO:0000313|Proteomes:UP000000787};
RN   [1] {ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC
RT   23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABX05266.1, ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RX   PubMed=22675585; DOI=10.4056/sigs.2194987;
RA   Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA   Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L., Han C.,
RA   Detter J.C., Schmutz J., Brettin T., Land M., Hauser L.,
RA   Kyrpides N.C., Ivanova N., Goker M., Woyke T., Klenk H.P.,
RA   Bryant D.A.;
RT   "Complete genome sequence of the filamentous gliding predatory
RT   bacterium Herpetosiphon aurantiacus type strain (114-95(T)).";
RL   Stand. Genomic Sci. 5:356-370(2011).
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DR   EMBL; CP000875; ABX05266.1; -; Genomic_DNA.
DR   STRING; 316274.Haur_2628; -.
DR   EnsemblBacteria; ABX05266; ABX05266; Haur_2628.
DR   KEGG; hau:Haur_2628; -.
DR   eggNOG; ENOG4108JIK; Bacteria.
DR   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008989; -.
DR   KO; K01968; -.
DR   OMA; AMKLEHP; -.
DR   BioCyc; HAUR316274:GHYA-2656-MONOMER; -.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   InterPro; IPR011761; ATP-grasp.
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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000313|EMBL:ABX05266.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000787};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000787}.
FT   DOMAIN        3    447       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      122    319       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      565    651       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   653 AA;  70814 MW;  05624C32E7F3B4D6 CRC64;
     MTYFDSLLIA NRGEIAVRVI RACRSLGIEA IAVYSDADAR ALHVREADRA IRIGPAAAAQ
     SYLNIEAVLA AAQQTGAQAI HPGYGFLSEN ANFARACQSA GIAFIGPPAE AIEAMGSKSA
     AKRLAESVGV PTVPGYNGDD QSEQRLLAEA ERIGFPLLIK ASAGGGGKGM RSVHRLAEFS
     AALAAAQREA LAAFGDQHVL LEKLIERPRH IEFQILGDQH GTMLHLGERE CSIQRRHQKV
     LEESPSIALT PALRATMGAA AVRLAQAVNY YNAGTQEFML DANGEFYFLE MNTRLQVEHP
     VTELVTGLDL VQLQIAIAAG QRLPFAQADI QQTGHAIEVR LYAEDPVQML PSIGQLSSYT
     PPEGPGIRLD TGVTVGDHVT INYDPMLAKL IVWGEQREQA IARLRYALQH FEVAGVTTNI
     PLLQAIINTP AYQAGATTTD FLQTYAISEQ LQHRQLPPNL ALAARALFDL EPDPDAALVG
     DPWNVPWRAA HMPHQLRYQS NDQTVPIKAQ PQAPQAWLVT INDEQLEIVV LRRHLNRMVV
     RVADRIYQCQ LEQDSLVWQG VGYQIQPAAA PSLDQNNGHK GDASLEAPMP GTIIKLLVAE
     GEHVSAGQPL LIMEAMKMEH TVTAPYAGTV AKLPYRQGQQ VSGGVALAEI TAE
//
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