ID A0A354K4H0_9FIRM Unreviewed; 1353 AA. AC A0A354K4H0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|HAMAP-Rule:MF_01210}; DE Includes: DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197}; DE AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197}; DE Includes: DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000256|HAMAP-Rule:MF_01210}; GN Synonyms=dapF {ECO:0000256|HAMAP-Rule:MF_00197}; GN ORFNames=DDX71_01265 {ECO:0000313|EMBL:HBI84908.1}; OS Ruminococcus sp. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=41978 {ECO:0000313|EMBL:HBI84908.1}; RN [1] {ECO:0000313|EMBL:HBI84908.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA9758 {ECO:0000313|EMBL:HBI84908.1}; RX PubMed=30148503; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 0:0-0(2018). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6- CC diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- CC DAP), a precursor of L-lysine and an essential component of the CC bacterial peptidoglycan. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:58359; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS00383240}; CC -!- CATALYTIC ACTIVITY: CC Reaction=LL-2,6-diaminoheptanedioate = meso-2,6-diaminopimelate; CC Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791; CC EC=5.1.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00197}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00611658}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step CC 1/1. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HBI84908.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DNTQ01000016; HBI84908.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00025. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR HAMAP; MF_00197; DAP_epimerase; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 2. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR TIGRFAMs; TIGR00652; DapF; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00197}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01210}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}; KW Manganese {ECO:0000256|SAAS:SAAS00511130}; KW Metal-binding {ECO:0000256|SAAS:SAAS00511109}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|PROSITE-ProRule:PRU00409}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01210}. FT DOMAIN 133 327 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 673 863 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 401 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 931 1353 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. FT REGION 1148 1149 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 1287 1288 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 1297 1298 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT ACT_SITE 1147 1147 {ECO:0000256|PROSITE-ProRule:PRU10125}. FT ACT_SITE 1147 1147 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT ACT_SITE 1296 1296 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 1087 1087 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 1138 1138 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 1236 1236 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT BINDING 1269 1269 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT SITE 1238 1238 Could be important to modulate the pK FT values of the two catalytic cysteine FT residues. {ECO:0000256|HAMAP-Rule: FT MF_00197}. FT SITE 1287 1287 Could be important to modulate the pK FT values of the two catalytic cysteine FT residues. {ECO:0000256|HAMAP-Rule: FT MF_00197}. SQ SEQUENCE 1353 AA; 146554 MW; 3F6C337DCDA041A9 CRC64; MPLNRDIHKV LVIGSGPIVI GQAAEFDYSG TQACRALKEE GIEVVLVNSN PATIMTDNQI ADQIYMEPLK SDVIKRICLK EKPDSILSGL GGQTGLNLCA ELAKSGFLAA NGIRLLGANP ETIARAEDRK LFKETMDSIG QPCIPSGIAE DMETARHIAA EIGYPVIIRP AYTLGGSGGG IAETPSDLEK IAENGLRLSP IHQILVERCI AGWKEIEFEI VRDADGNKLT VCSMENFDPV GIHTGDSIVI APAVTLADKE YQMLRTAALK IAEVLKIEGG CNCQFALSPD SFEYAVIEVN PRVSRSSALA SKATGYPIAK VAAKIAIGYR LYEIANKVTG KTTAAFEPSL DYVAVKMPKF PFEKFASASH RLGTQMKATG EVMAISDSFE SALLKALRGA EVKHSALLVR ALRSLPDAEL REHLVHADDV RLFAAAEAMR RGFSVDEIAE ASRIDRWFLH KICKLVTCET ALENTPLTDA LYRTAKRFGY PDDTIAAISD KALPEKRYRP HYRMVDTCAG EFAAETPYFY GVCKPDAAQE ADEAAAFLAG RPHKTVVVLG SGPIRIGQGI EFDYSAVHCV QVLKNAGYEV VLINNNPETV STDFDTADRL YFEPLTPEDV LSILALEQPV GVVTAFGGQT AIRLARTIEE AGYRLLGASA DSIDLAEDRE RFDALLESLQ IDRPRGCTVD TLEEAAEAVQ TLGLPVLVRP SYVLGGQNMN IAFESGDVAA FMQNILADGI DNPVLIDQYI RGTEIEVDAI CDGKDILIPG IMEHIERTGV HSGDSIAICP PVHIDDEMRR KILTDTKKIC LGLHAVGLIN LQYIVKGHSL YVIEVNPRAS RTVPFMSKLT GLPLCDCAMR VCLGEKLAAM DYGTGYYKTP PYTAVKVPVF SFEKIGGESQ LGPEMKSTGE VIGIGKTLTE ALYKGLRAAG YRLEDSGRNG SGVLLTVCDA DKPDIVEIAR KFARLGFVLY ATSGTAAALT RAGLAVHTLR KLHDGDTETF RLMENGTIRY IVSTDANARM AARDGAKIRK KAVELGIPCL TCTDTAAAVA NCLHTGYRDS NVELMNMNHL RTAKRRIPFV KMHGCGNDYI YVNCMEKRVS APESLAVQLS DRHFGIGGDG LVLIESSEIA DARMRMFNLD GSEGNMCGNA IRCVAKYLYD NGICTKKEIV IETKSGLRTV TVTTQNGVVT HAAVNMGKAI FEPARIPVQF AGNEMIAQPL TVAGTEYTVT CVSMGNPHCV VFGENPETLN LAAIGPEFEH HPAFPEQVNT EFVQVINRKT LRMRVWERGS GETMACGTGA CGTVAAAVKN GFCDPDTDVT VHLNGGDLVI RYTEDAVFMT GEAVLIFSGE IEV //