ID A0A150AKB4_9BACT Unreviewed; 812 AA.
AC A0A150AKB4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AVL50_12070 {ECO:0000313|EMBL:KXX70336.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX70336.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX70336.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX70336.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KXX70336.1}.
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DR EMBL; LQAQ01000060; KXX70336.1; -; Genomic_DNA.
DR RefSeq; WP_062616857.1; NZ_LQAQ01000060.1.
DR AlphaFoldDB; A0A150AKB4; -.
DR STRING; 1775430.AVL50_12070; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000075267; 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:UP000075267}.
FT DOMAIN 685..809
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 478
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 706
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 577
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 755
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 478
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 812 AA; 92386 MW; D3C7EA190729110F CRC64;
MPQSELDFST SFWNAEYLLI DSRQLSAPSN TIFFALDGKK RTGQSFIPEL YEKGVRKFVV
TSAFDKAYLY KEATFVYTEN TLTTLQQLTA WHRTQHQQLP AISITGSNAK TIVKEWLYFL
LEMDYNVVKS PKSYNSQIGV PLSIWQINDK HDLGIFEAGI SQPNEMEKLE KIIQPNIGLF
TNIGTAHDKD FDTLEQKIDE KAKLFKNCEI VVYCKDHPLI DEKLMALELP TFSWGEHPDA
DLKIMKVADY EIMVNYEGET FPMNIPFLDD ASFENVMHCV AILVCLEYPF ETINSRINKL
KRIPMRLERK EGINNTVLIN DFYNNDLGGL QIALSFLSQN QEKYPRTLIF SDLLQGDKDK
KALYERVNQL CKEYKIDKFV GVGEQLQSFE KVFQINEKCF YSNTNEVRKA IKNGELHFNK
ELILLKGARQ FEFEKIATLL QKKIHSTQLE INLDAVVHNL MFYRSQLSPQ TKVMVMVKAL
GYGSGKSELA NILQYHLVDY LGVAFADEGV ELRENGIRTP IMVLTPSPDS FEMMRMHQLE
PEIYNIEMLS ALEKFIAEEN HDEPFAIQIN FDTGMHRLGF TSDNYDELEE RLLKLSDKIS
VKGAFTHLAG ADESIHDSYS KNQIKEFQQL TSKLENALGY HVIKHCLNSA GIVRYPKAQM
DMVRLGIGLH GVEVNNLKQD DLQPVATLKT VIAQIKEMKK GETVGYSRKG KVEAPKKIAT
IGIGYADGFD RRLSNGVGKV VINGQLAPVI GNVCMDMTMV DISDITANVG DEVIVFGEDR
SISTIAKEIG TIPYEILTSV SSRVKRIYYM EG
//
