ID A0A354K4H0_9FIRM Unreviewed; 1353 AA. AC A0A354K4H0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 17-JUN-2020, entry version 10. 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, ECO:0000313|Proteomes:UP000262685}; RN [1] {ECO:0000313|EMBL:HBI84908.1, ECO:0000313|Proteomes:UP000262685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9758 {ECO:0000313|EMBL:HBI84908.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; 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 substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- CC lysine and an essential component of the bacterial peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, CC ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000256|HAMAP- CC 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:58228, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00611658}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP- CC 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 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|HAMAP- CC 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 the CC 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 of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 Proteomes; UP000262685; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. 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:SAAS00459951}; KW Metal-binding {ECO:0000256|SAAS:SAAS00086100}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01210}. FT DOMAIN 133..327 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 673..863 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 1..401 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 931..1353 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 1148..1149 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 1287..1288 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT REGION 1297..1298 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 1147 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10125" FT ACT_SITE 1147 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT ACT_SITE 1296 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 1087 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 1138 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 1236 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT BINDING 1269 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 1238 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197" FT SITE 1287 FT /note="Could be important to modulate the pK values of the FT two catalytic cysteine residues" FT /evidence="ECO:0000256|HAMAP-Rule: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 //