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}.
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; 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
//