ID A0A086B0M8_9FLAO Unreviewed; 815 AA.
AC A0A086B0M8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=IW22_04750 {ECO:0000313|EMBL:KFF22492.1};
OS Chryseobacterium sp. JM1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233950 {ECO:0000313|EMBL:KFF22492.1, ECO:0000313|Proteomes:UP000028731};
RN [1] {ECO:0000313|EMBL:KFF22492.1, ECO:0000313|Proteomes:UP000028731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM1 {ECO:0000313|EMBL:KFF22492.1,
RC ECO:0000313|Proteomes:UP000028731};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Chryseobacterium sp. JM1.";
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:KFF22492.1}.
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DR EMBL; JPRN01000002; KFF22492.1; -; Genomic_DNA.
DR RefSeq; WP_034724450.1; NZ_JPRN01000002.1.
DR AlphaFoldDB; A0A086B0M8; -.
DR eggNOG; COG0770; Bacteria.
DR eggNOG; COG0787; Bacteria.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000028731; 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}.
FT DOMAIN 688..813
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 483
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 709
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 582
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 758
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 483
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 815 AA; 92644 MW; 8BBCDEB7DED7D890 CRC64;
MNYTVKQIAD ITNAQIIGDK DLVIRNIAFD SRIIYSTKNT AFVAINTHKN SGEKFIESAI
DRGIAVIISE HQYPQFENIT WIIVENSVDF LQQLAKYHFE NAHLKSIGIT GSNGKTILKE
WLYQCLWNEF PTVKSPKSFN SQIGLPLSLL QINSSYELGI FEVGISKPHE MEKLEHIFHP
QIGLLTHIGN AHAANFQSEE ELIDEKIMLF KGSEVIIYNG DNALVDQKIK TLYSDKKLIS
YGFKNNNQVF IKENISKDEK ITVVYFDEEI SFPVHQRDEA TLTNALALIT VLKELNIDNQ
KIIEKINSLK AVEMRLEAIE GIKNNIVIND SFNLDLDSLK TALQFLNEYK KSKKSLVLTD
IVGVNSNSEE LYEEVSELVN DQNFDSVFLI GDEISKFSEL FKAKTSTFVN TKELIDSKRL
TEIENQIILL KGARKFEIEK LKDILELRKH DTVLEINLNA ILHNINYHKS LLKPETKMMA
MVKANAYGLG SYEISEFLQH HHIDYLGVAY ADEGVELRKK GITTPIVVMN PEQHSYEAII
EYNLEPEIYS FRVLELFYEA VQKSGYDKKY PIHIKLETGM HRLGFKDFEL DQLSETLSSK
NVKVQSLFSH LSSSDMPEEK EFTFRQFEVF EKNSSYLIEK LGYAPIRHIL NSSGITSYTE
QQYDMVRIGI GMIGESPCSE IQKQLQSVVS FKTVISQIST VDTGESVGYS RKYKPDHAAK
IATIPVGYAD GIPRLIGNQV GNVGVNKILA PIVGNICMDM MMINVDQIPN VKEGDTVTVF
NAKPSLKEFA GYCKTITYEV LTSISPRVKR IYIKD
//
