ID A0A0C1I529_9BACT Unreviewed; 824 AA.
AC A0A0C1I529;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=HY58_18330 {ECO:0000313|EMBL:KIC89210.1};
OS Flavihumibacter sp. ZG627.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC89210.1, ECO:0000313|Proteomes:UP000031400};
RN [1] {ECO:0000313|EMBL:KIC89210.1, ECO:0000313|Proteomes:UP000031400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC89210.1,
RC ECO:0000313|Proteomes:UP000031400};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter carbonis ZG627.";
RL Submitted (JUL-2014) 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:KIC89210.1}.
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DR EMBL; JPHF01000013; KIC89210.1; -; Genomic_DNA.
DR RefSeq; WP_039135270.1; NZ_JPHF01000013.1.
DR AlphaFoldDB; A0A0C1I529; -.
DR STRING; 1463156.HY58_18330; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000031400; 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; 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; 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:UP000031400}.
FT DOMAIN 697..822
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 493
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 718
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 591
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 493
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 824 AA; 92014 MW; A06FB87B70184009 CRC64;
MQYTIPDIAA IIGARWQRQA GSATISHLLI DSRKLLFPQS TVFFALKTES RNGHQFIGRL
YQQGVRCFVV SEEMDPKTFP GASLLLVENT LIALQTLAAA HRKKFSYPVI GITGSNGKTI
VKEWLNQLLE EDHNIVRSPR SYNSQIGVPL SVWQMGRLHS LGIFEAGISR TEEMLALQNI
IQPTIGILTN IGAAHNEGFS SLRQKLEEKW KLFHSAGVII YKRDHGLTDE YVNEIRRDDC
LYFSWSFEGD ATMQVSRTGA DETGVECTIR YQDQTFALRI PFTDEASIEN ALTCCACLLY
MDLPADLITK RIAQLHSVGM RLEMKEGINH CSVINDSYSA DLSSLIIALD FLAQQKQHLT
KTVILSDIPE TGMPEEELYQ RVAMLLQHHG VKKLFAIGPR ISAHKAVFEA AALEVHSYPE
TASFIAHAPE IHFRDETILI KGARRFSFED ISALLEMQVH QTVLEINLNA MLQNLKQYQQ
LLQPSTRLMA MVKAFSYGSG SYEIASLLQF HGVDYLAVAY TDEGVALRKA GIDMPIMVMN
ASPSAFDALV EFNLEPVLYS LQLYKRFAAY IRQQAITRYP VHLEMETGMN RLGFEEADIK
ELLQLLVQPW FKIQSVFSHL AASEDPQHDG FTHQQVELFE AATKRIAAVL DHSFLKHIEN
TAAIFRHPQW QMDMVRLGIG LYGVDPSASS AMRLEEVSTL RTTIAQIKEL APGETVGYGR
RGVAARQTRI ATVRIGYADG YPRVLGNGRG SMLVGNQLAP VIGSICMDMT MIDITGIDGI
EEGDEVIVFG KGLPVAELAA AAGTIPYEIM TGVSQRVKRI YYLD
//
