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Entry: C5BRB1_TERTT
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ID   C5BRB1_TERTT            Unreviewed;      1201 AA.
AC   C5BRB1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-JUN-2014, entry version 38.
DE   SubName: Full=Urea carboxylase;
DE            EC=6.3.4.6;
GN   Name=uca; OrderedLocusNames=TERTU_3485;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadales genera incertae sedis; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J.,
RA   Madinger C., Nove J., Anton B., Chaudhary K., Foster J., Holman A.,
RA   Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B.,
RA   Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA   Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an
RT   intracellular endosymbiont of marine wood-boring bivalves
RT   (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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DR   EMBL; CP001614; ACR13946.1; -; Genomic_DNA.
DR   RefSeq; YP_003074818.1; NC_012997.1.
DR   ProteinModelPortal; C5BRB1; -.
DR   STRING; 377629.TERTU_3485; -.
DR   EnsemblBacteria; ACR13946; ACR13946; TERTU_3485.
DR   GeneID; 8214146; -.
DR   KEGG; ttu:TERTU_3485; -.
DR   PATRIC; 23873853; VBITerTur118718_3250.
DR   eggNOG; COG0511; -.
DR   HOGENOM; HOG000251581; -.
DR   KO; K01941; -.
DR   OMA; VEWMVRQ; -.
DR   OrthoDB; EOG6CVV6Z; -.
DR   BioCyc; TTUR377629:GHSU-3162-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 2.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR003833; Allophan_hydro_1.
DR   InterPro; IPR003778; Allophan_hydro_2.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR014084; Urea_COase.
DR   Pfam; PF02682; AHS1; 1.
DR   Pfam; PF02626; AHS2; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SMART; SM00797; AHS2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF50891; SSF50891; 2.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00724; urea_amlyse_rel; 1.
DR   TIGRFAMs; TIGR02712; urea_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   Complete proteome; Ligase.
SQ   SEQUENCE   1201 AA;  131280 MW;  5E6C561DB174B99D CRC64;
     MFNKILIANR GAISTRISRT LNTMGVASVA VYSEADAHSL HVTAADEAYS LGEGGAAETY
     LNTEKLFAIM AQAGVDAVHP GYGFLSENAD FVAECDKRNI AFIGPRPEHM QAFGLKHEAR
     ALAVAQQVPL LPGSDLLDSE DEALLAAATI GYPIILKSTA GGGGIGMQVC KDAAELQKNF
     ASVKRLGANN FANDGVFIEK YIEFARHIEV QVFGDGAGNA VAFGERDCSA QRRHQKVIEE
     TPAPNIPDDV RSQLHLTATK LLAAVNYLNA GTVEFIYDQN THQFYFLEVN TRLQVEHGVT
     EEVFKVDLVA WMVRQAAGEL GDITKLRAQL APQGHAIQAR VYAEDPHKNF QPSAGLLSCV
     ALPDNTSQRR IDHWIETGLE VSAFFDPMLA KFICRADSRE AAIAELSAAL SASRIQGIET
     NMAYLCDLLD DPVLLEGRLY TRYLNNRSFV PQTMDVLSGG TLTTLQDFPG RTGYWDVGVP
     PSGPFDNLAL RLANAALGNP ADAAGLEITL QGPTLRFNCA TQFILTGADF SAELDAEPLQ
     SYRVYAATAG QVLRIGQPLG AGARAYLAVA GGLDGNVYLG SRSTFTLGQF GGHSGRALRT
     GDVLHFAQGA SAIAADNIQH LKPTVNTDWN IRVIYGPHGA PDFFTEKDIA TFFNSDWKIH
     YNSSRTGIRL IGPKPDWART TGGEAGMHPS NIHDNAYAVG TIDFTGDMPV ILGPDGPSLG
     GFVCPATVIK ADLWKLGQLK AGDRVRFTPV NLATAEKLER HQLACCTQLT ASAEPLYSSE
     DIATASPVLH RLSEQENAVE VCYRLAGDDY LLVEYGPQQL DIALRFRAHA LMLKLQELNH
     PAIMELTPGI RSLQIHYDNL ALPAQALLQL LLSAERALKD VEQQRIAARV VHLPLSWNDQ
     ACQLAVQKYT QSVRKDAPWC PDNIEFIRRI NGLDSVDDVK RIVFDASYVV MGLGDVYLGA
     PVATPLDPRH RLVTTKYNPA RTWTAENSVG IGGAYLCVYG MEGPGGYQFI GRTLQMWNKN
     KTTREFSRPW LLRFFDQIRF YEVSEEELID IRRRFPHGDY PLKIEDTEFS LADYQAFLTQ
     HQTSIDNFVE QRQTAFDEEL ARWISSGQMN FDATTTSAPA EDEAPLAANC TALESPAAGS
     LWQWCVAEGE TVNEGDVVCI LESMKMEIEI YAPAAGTLLK QQRHQGDVIA AGQTLGVISH
     A
//
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