ID A0A180ESA8_9BACT Unreviewed; 792 AA.
AC A0A180ESA8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A3850_018025 {ECO:0000313|EMBL:OAV46158.1};
OS Lewinella sp. 4G2.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Lewinella.
OX NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV46158.1, ECO:0000313|Proteomes:UP000076582};
RN [1] {ECO:0000313|EMBL:OAV46158.1, ECO:0000313|Proteomes:UP000076582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G2 {ECO:0000313|EMBL:OAV46158.1,
RC ECO:0000313|Proteomes:UP000076582};
RA Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., Hamasaki K.;
RT "Lewinella sp. 4G2 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 -!- 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:OAV46158.1}.
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DR EMBL; LVWJ02000011; OAV46158.1; -; Genomic_DNA.
DR RefSeq; WP_068212974.1; NZ_LVWJ02000011.1.
DR AlphaFoldDB; A0A180ESA8; -.
DR STRING; 1803372.A3850_018025; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000076582; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
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:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000076582}.
FT DOMAIN 663..790
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 468
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 684
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 559
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 468
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 792 AA; 86603 MW; C7F482961E22B3BC CRC64;
MEANYHPDNL AELYACYAGF DLVVDSRRVT RPKQTLFFAL PGRKTHGVSF VEDLGKAGVE
HFVIPISHKN EALPQVLNMD GAHRVTFATD PVEVLQALAA HHRAQFDIPV VGITGSNGKT
IVKDWLSQIL SKQFKVCASP RSYNSQIGVP LSVWQLRPEH EVAVFEAGVS ATGEMGKLAR
IIQPTLGVFT HFGAAHDDGF ANREEKLREK LSLFSATQFV VVNEAHREVR KALKGSNLEL
VHQGNGLDQL VIDGRELDIA LPKLPRIYRE NAYSALTAAY WLGMEPEALR NASSKLLPLK
NRLEQTAGLH GGPVINDSYS NDLDALAAAL QFAANQGSSG KVQLILGSLQ PYHLPTSPGT
RGSALMNLLE EYVDTLMLVG DEHEAGIRDR ATATFPTTEA LLNGLDELAF NSLPILVKGA
SHQQLGRVAK ALSRHQHRTN LRIDLGAIQH NFRTYQQRVD AKMIVMVKAS AYGGGSLPIA
RAVAEAGADY LAVAYTDEGR ELRRGGVQLP IMVLNPEREE FAEMLDFDLE PVVASVNDLR
HAGELGLPVH WELDTGMARL GMPLEKAADS IRFAPKMPVV NSIFTHLVAS EATEHDHFTR
EQFAGFQREA RRITSALGYT PLLHVLNSNG IARWPKLQLD AVRLGIGLYG IGDATLATEL
QPALRLTTRV ALLRNYPAGT TIGYNRRGIL KRDSLIATLS IGYADGLPRL AGEGEFSVLI
NGQAAPTVGA VCMDMTMVDV TDHDPHLLRE GIEAVIFGPE HPVELLAAAA RTIPYEILTG
IGQRVHRIYV RE
//
