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Database: UniProt/TrEMBL
Entry: A0A1A9I6J8_9BACT
LinkDB: A0A1A9I6J8_9BACT
Original site: A0A1A9I6J8_9BACT 
ID   A0A1A9I6J8_9BACT        Unreviewed;       827 AA.
AC   A0A1A9I6J8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=A8C56_19940 {ECO:0000313|EMBL:ANH82955.1};
OS   Niabella ginsenosidivorans.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=1176587 {ECO:0000313|EMBL:ANH82955.1, ECO:0000313|Proteomes:UP000077667};
RN   [1] {ECO:0000313|EMBL:ANH82955.1, ECO:0000313|Proteomes:UP000077667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS26 {ECO:0000313|EMBL:ANH82955.1,
RC   ECO:0000313|Proteomes:UP000077667};
RA   Im W.T., Siddiqi M.Z.;
RT   "Niabella ginsenosidivorans BS26 whole genome sequencing.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP015772; ANH82955.1; -; Genomic_DNA.
DR   RefSeq; WP_067760007.1; NZ_CP015772.1.
DR   AlphaFoldDB; A0A1A9I6J8; -.
DR   STRING; 1176587.A8C56_19940; -.
DR   KEGG; nia:A8C56_19940; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000077667; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
DR   NCBIfam; TIGR00492; alr; 1.
DR   NCBIfam; TIGR01143; murF; 1.
DR   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Ligase {ECO:0000313|EMBL:ANH82955.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000077667}.
FT   DOMAIN          699..824
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        496
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        720
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         594
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         769
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         496
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   827 AA;  92083 MW;  96CBABFE1AF604BB CRC64;
     MVNPGYSIQQ IAAILGLQNI PDVNKGFVNT LLTDSRKLTS PSTSLFFALQ GPQRNGHVFV
     PELYKKGVRF FVISRDIDET LYPGSVFFKV ADPLQSLQKI AAAHRHRFAV DVIGITGSNG
     KTVVKEWLYQ LLQPYKNIVR SPKSYNSQLG VPLSIWQMSP ENDLAVFEAG ISKPGEMEQL
     QEIIDPTIGV LTNIGLAHSE GFVNDAQKLS EKLQLFKTAK VVIANGDSEL ITWGARQLNR
     PLFSWGKAAH NNVQVLAVHT TGAYAVIRLK EKEGSDFNIE IPFSDNASVE NAIICATVLL
     YLKFAPSVIA SGMKALQPVN MRMEFKQGIN NCVIINDSYS ADLTSLEVAL QFLQQQSKGK
     KKTVILSDFF ENDANDRQLY QSIYQLLKRY DINRLIGIGE KMQLLFPLLL TEEETMEASF
     FLSTKKYLQQ YHSTQYRDEY ILVKGARRFG FERIVTLLEQ KVHETVLEIN LDAVAHNLKA
     FQQLLKPGVK LMAMVKAFAY GSGAAEIASV VQFHKADYLG VAYADEGVEL RKAGITIPIM
     VLNVEESAFD AITDYNLEPD IFSFELLNAF EQHIKSAGLK NYPVHIEVET GMNRSGFAVA
     DISVLADRLT GNEFIKVQSC FSHLAASEDK VEDAFTLHQF ELLKKATDIL EAGLSYTFIR
     HIANTSAIMR FPELQLDMVR LGIGLYGIAG NDKIPLQTVA TLKTTISQIK RIRNGETVSY
     NRRGIAKEDS VIATIRIGYA DGYSRRLGNG VGKVWVNGQL APVIGTVCMD MTMIDITHIP
     EVKEGDDVIV FGEAVPVQQL AEWIGTIPYE IMTGISQRVK RVYYGEG
//
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