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Multifunctional fusion protein [Includes: Diaminopimelate epimerase (DAP epimerase) (EC 5.1.1.7) (PLP-independent amino acid racemase); Carbamoyl-phosphate synthase large chain (EC 6.3.5.5) (Carbamoyl-phosphate synthetase ammonia chain)]

 U1GRY7_TRESO            Unreviewed;      1402 AA.
U1GRY7;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
22-NOV-2017, entry version 33.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|HAMAP-Rule:MF_01210};
Includes:
RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197};
AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
Includes:
RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
Synonyms=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
ORFNames=HMPREF1325_0913 {ECO:0000313|EMBL:ERF59429.1};
Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF59429.1, ECO:0000313|Proteomes:UP000016412};
[1] {ECO:0000313|EMBL:ERF59429.1, ECO:0000313|Proteomes:UP000016412}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF59429.1,
ECO:0000313|Proteomes:UP000016412};
Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
Haft D.H., Methe B., Sutton G., Nelson K.E.;
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-
diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-
DAP), a precursor of L-lysine and an essential component of the
bacterial peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00197}.
-!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
ADP + phosphate + L-glutamate + carbamoyl phosphate.
{ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00383240}.
-!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00197}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00611658};
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
carbamoyl phosphate from bicarbonate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01210}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step
1/1. {ECO:0000256|HAMAP-Rule:MF_00197}.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
{ECO:0000256|HAMAP-Rule:MF_01210}.
-!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
promotes the hydrolysis of glutamine to ammonia, which is used by
the large (or ammonia) chain to synthesize carbamoyl phosphate.
{ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
-!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
-!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
{ECO:0000256|HAMAP-Rule:MF_00197}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ERF59429.1}.
-----------------------------------------------------------------------
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EMBL; AUZJ01000071; ERF59429.1; -; Genomic_DNA.
EnsemblBacteria; ERF59429; ERF59429; HMPREF1325_0913.
PATRIC; fig|1125725.3.peg.2665; -.
OrthoDB; POG091H01IP; -.
UniPathway; UPA00034; UER00025.
UniPathway; UPA00068; UER00171.
UniPathway; UPA00070; UER00115.
Proteomes; UP000016412; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
Gene3D; 1.10.1030.10; -; 1.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.1380; -; 1.
HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
HAMAP; MF_00197; DAP_epimerase; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR006275; CarbamoylP_synth_lsu.
InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
InterPro; IPR001653; DAP_epimerase_DapF.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF02786; CPSase_L_D2; 2.
Pfam; PF02787; CPSase_L_D3; 1.
Pfam; PF01678; DAP_epimerase; 2.
Pfam; PF02142; MGS; 1.
PRINTS; PR00098; CPSASE.
SMART; SM01096; CPSase_L_D3; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF48108; SSF48108; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF52440; SSF52440; 2.
TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
TIGRFAMs; TIGR00652; DapF; 1.
PROSITE; PS50975; ATP_GRASP; 2.
PROSITE; PS00867; CPSASE_2; 2.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197,
ECO:0000256|HAMAP-Rule:MF_01210};
Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
ProRule:PRU00409};
Complete proteome {ECO:0000313|Proteomes:UP000016412};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00197,
ECO:0000313|EMBL:ERF59429.1};
Ligase {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000313|EMBL:ERF59429.1};
Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
Manganese {ECO:0000256|SAAS:SAAS00511130};
Metal-binding {ECO:0000256|SAAS:SAAS00511109};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
ECO:0000256|PROSITE-ProRule:PRU00409};
Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
Reference proteome {ECO:0000313|Proteomes:UP000016412};
Repeat {ECO:0000256|HAMAP-Rule:MF_01210}.
DOMAIN 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
DOMAIN 700 890 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
REGION 1 402 Carboxyphosphate synthetic domain.
{ECO:0000256|HAMAP-Rule:MF_01210}.
REGION 959 1402 Allosteric domain. {ECO:0000256|HAMAP-
Rule:MF_01210}.
REGION 1173 1174 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
REGION 1336 1337 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
REGION 1346 1347 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
ACT_SITE 1345 1345 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1112 1112 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1163 1163 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1318 1318 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SITE 1287 1287 Could be important to modulate the pK
values of the two catalytic cysteine
residues. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SITE 1336 1336 Could be important to modulate the pK
values of the two catalytic cysteine
residues. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SEQUENCE 1402 AA; 152859 MW; 87141E64A78732FF CRC64;
MPLNTSIRKV MVIGSGPIVI GQAVEFDYAG TQACKALKEQ GLSVVLVNSN PATLMTDRSM
ADAVYIEPLI PETIRRIIEK EKPDSLLSTL GGQTGLTLSM ELAKSGFLKS HGVQLLGARP
DTIDKAEDRQ IFKDTMLSIG EPCIPSKVVT TLEDAVDFAE HEIGYPAIVR PAFTLGGTGG
GIAETKSELE EIAQNGLHRS PIHQILVEKC IAGWKEIEFE VVRDHSGNAI TVCSMENVDP
VGIHTGDSIV VAPTMTLSDK EYQMLRSASF NIVGSLGMEG GCNVQFALHP STSEYAVIEV
NPRVSRSSAL ASKATGYPIA RVATLIAIGY NLDEIPNFVT KKTSAYFEPV VDYVVVKMPK
FPFDKFVYAK RTLGTQMKAT GEVMSIGRTF EEAIMKAVRG AEIGTDSMRL KQFVNESDER
IKERIGECTD RRIFAIYEAL VRGIMSIDEI NKITKIDIWF LAKLQHIAFR ELELASVKTG
KQKLSPLLYL EAKKDGFPDK TITELSGVAI PGGSGIIKEA KDAAALVKQG KLAHIPATYK
MVDTCTGEFS AETPYFYGGY YEENEAADFL AEHAKSKSKK GTIIVLGSGP IRIGQGIEFD
YASVQCVWSL KKLGYDVVTI NNNPETVSTD FDTSDRLYFE PLTPEDVMSV INTEKPIGVV
VAFGGQTAIK LTKFLDEQGI KILGTSAESI DIAEDREKFE ALCVKLGINK PAGETVLTTE
EAIASAQRIG YPILLRPSYV LGGQNMIIAW GDADVREYMG IILSQGIENP VLIDKYMGGT
ELEVDAICDG KDILIPGIME HIERAGIHSG DSIAVYPSWN LNDILRQKII KQSRELALAL
GTKGLVNIQY LIYNNDLYVI EVNPRSSRTV PYISKVTGVP MVELAVRAML GEKVKTFGYG
TGLYRISPYF AVKVPVFSFE KLMDVDTHLG PEMKSTGEVL GLASTMEEAI YKGLIGAGYR
MKRSGGVLFT VRKTDQFEIP DLARKFYDMG FTLYATEGTA GVIKDFGMEV TVVNKIHENP
DDNLLTLLDT GKIDYVISTS TKGRDPHADS VRMRRHAVER DIPCLTAIDT ANAIANCLMS
HYNAENVELV DINALRESKE KLRFCKMQST GNDFILIDAR KQAVANPAGL AVRLCNRRME
IGADSLVLVK DSDKADAYMQ FFNQDGSEGR LAGNAIRSVA KYLYDNNING VKDRGDAASP
TASLSIDTAS GTKSLVLYKL DGKVSSVTVD MGRPLFDAAS LPTTLSPVST SRESLAARIP
QKAIVNVPLT VDGTKYDVTC LSVGTPHCVV FCGFVDKVDV EKIGPLFENN AVFPNRTNTE
FVRVVGRNEL KMRTWERGNG ETPACGTGAC AAAIAAVLNG YCPMDENITV QVKGGTLIVK
YTGDTVYLTG QSDTVYEGEI EI


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