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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)]

 F2NU25_TRES6            Unreviewed;      1411 AA.
F2NU25;
31-MAY-2011, integrated into UniProtKB/TrEMBL.
31-MAY-2011, sequence version 1.
18-JUL-2018, entry version 60.
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=dapF {ECO:0000256|HAMAP-Rule:MF_00197};
Synonyms=carB {ECO:0000256|HAMAP-Rule:MF_01210};
OrderedLocusNames=Tresu_0019 {ECO:0000313|EMBL:AEB12989.1};
Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB12989.1, ECO:0000313|Proteomes:UP000006852};
[1] {ECO:0000313|Proteomes:UP000006852}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33096 / DSM 2489 / 6091
{ECO:0000313|Proteomes:UP000006852};
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of chromosome of Treponema succinifaciens DSM
2489.";
Submitted (APR-2011) 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, ECO:0000256|SAAS:SAAS01000080}.
-!- 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_00197}.
-----------------------------------------------------------------------
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EMBL; CP002631; AEB12989.1; -; Genomic_DNA.
STRING; 869209.Tresu_0019; -.
EnsemblBacteria; AEB12989; AEB12989; Tresu_0019.
KEGG; tsu:Tresu_0019; -.
eggNOG; ENOG4105CU6; Bacteria.
eggNOG; COG0253; LUCA.
eggNOG; COG0458; LUCA.
KO; K01955; -.
OMA; AVFPFNK; -.
OrthoDB; POG091H01IP; -.
UniPathway; UPA00034; UER00025.
UniPathway; UPA00068; UER00171.
UniPathway; UPA00070; UER00115.
Proteomes; UP000006852; Chromosome.
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; 3.40.50.1380; -; 1.
HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
HAMAP; MF_00197; DAP_epimerase; 1.
InterPro; IPR011761; ATP-grasp.
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:UP000006852};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00197,
ECO:0000313|EMBL:AEB12989.1};
Ligase {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000313|EMBL:AEB12989.1};
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,
ECO:0000256|SAAS:SAAS01000143};
Reference proteome {ECO:0000313|Proteomes:UP000006852};
Repeat {ECO:0000256|HAMAP-Rule:MF_01210}.
DOMAIN 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
DOMAIN 702 892 ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
REGION 1 402 Carboxyphosphate synthetic domain.
{ECO:0000256|HAMAP-Rule:MF_01210}.
REGION 961 1411 Allosteric domain. {ECO:0000256|HAMAP-
Rule:MF_01210}.
REGION 1176 1177 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
REGION 1345 1346 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
REGION 1355 1356 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00197}.
ACT_SITE 1354 1354 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1114 1114 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1166 1166 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1294 1294 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
BINDING 1327 1327 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SITE 1296 1296 Could be important to modulate the pK
values of the two catalytic cysteine
residues. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SITE 1345 1345 Could be important to modulate the pK
values of the two catalytic cysteine
residues. {ECO:0000256|HAMAP-
Rule:MF_00197}.
SEQUENCE 1411 AA; 154963 MW; 2A0249CB3397CC59 CRC64;
MPLNKDIHKV MVIGSGPIII GQAAEFDYAG SQACKALKEQ GLEVVLVNSN PATLMTDHTM
ADQIYIEPLI PETIQRIIEK EKPDSLLSTL GGQTGLTLSM ELAKSGFLEN HGVKLLGAKP
ETIDKAEDRQ MFKDTMLAIG EPCIPSKVVT TYEDALDFVK NEIGYPAIIR PAFTLGGTGG
GIVHNDEEMD EIAHNGLHRS PIHQILVEKC ISGWKEIEFE VMRDSAGNVL TVCSMENFDP
VGVHTGDSIV IAPTVTLSDK EYQMLRSAAL NIISSLGMEG GCNCQFALNP NSFEYAVIEV
NPRVSRSSAL ASKATGYPIA KVATLIAIGY TLDEIPNAVT KKTAACFEPV LDYVVVKMPK
FPFDKFVYAK RDLGTQMKAT GEVMAIGQTF EQAIMKAVRG AEVGAQSLNL SSFVEMSDEE
IEKRVGECTD QRIFAIFQAI KRNILSIIQI NKITKIDLWF LAKLENLAFM ERDFAKVKAG
EKEFTPELYK AAKNAGYPDK VIQELAGQKI TGASGILSEA KEAAKLVKQG KVAHIPAVYK
MVDTCAGEFN AETPYFYGTY DSQNEARIFL DERKEKGKKS SKGTIIVLGS GPIRIGQGIE
FDYASVQCVW ALKRLGYDVV TINNNPETVS TDFDTSDRLY FEPLTPEDVM SVVNTEKPVG
VVVAFGGQTA IKLTKFLDSQ GIRILGTSAD SIDLAEDRER FEELCEKLHI NRPKGLTIFT
EEEALEATQK LGYPVLLRPS YVLGGQNMII AFNDDDVKEY MKIILAQGIE NPVLIDQYMM
GTELEVDAIC DGKDILIPGI MEHIERTGIH SGDSIAVYPS WNLNDILREK IINQSRELAL
ALGTKGLVNI QYLIYNNDLY IIEVNPRSSR TVPYISKVTN VPMVDLAVRA MLGEKVKNMG
FGTGLYRLPP YFAVKVPVFS FEKLMDVDTH LGPEMKSTGE VLGIASTMEE AIFKGLIGAG
YNMKRSGGVL FSVRKTDRYE LPDLAKKFYD MGFKLYATEG NAKTISDFGM EVEVVNKIHE
NPNDNLLSLL DSGKVDYVIS TSAKGRDPRA DSVRMRRHAV ERDIPCLTAI DTANAIANCL
KSKYTAENVE LVDINQLREE KQKITFYKMD STGNDFIVIN AMNQVVKNPA GLAVRLCDRR
NGGIGADSLV LIEESKIADA KMRFFNLDGT EGKMAGNAIR CVGKYLYDNN IKGIQEKHGK
KTDATEKITI ETGSGVKTLV LYKQNGKVTS VTVDMGKPLF ASEEIPTSLV AVDITNCGFN
EENKNAVLPK KAVVNAPLIV AGNEYRVTCI NVGNPHCVVF SKFVDKEPVT KIGPLFESHL
VFPEKTNTEF VRVVGPNELK MRTWERGNGE TLACGTGACA AAVASVINGF SPINQDITVK
VRGGNLIVKY TGETVLLTGN TKMCYQGEVE I


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