ID A0A0N0KB10_9SPHN Unreviewed; 424 AA.
AC A0A0N0KB10;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=IP83_07070 {ECO:0000313|EMBL:KPF87538.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF87538.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF87538.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF87538.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000316};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
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:KPF87538.1}.
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DR EMBL; LJHZ01000030; KPF87538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0KB10; -.
DR STRING; 1523427.IP83_07070; -.
DR PATRIC; fig|1523427.4.peg.2211; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000037906; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine 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; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR006311; TAT_signal.
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 PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..424
FT /note="alanine racemase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005853336"
FT DOMAIN 282..422
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 75
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 424 AA; 45634 MW; 0789D9F8EF9515F1 CRC64;
MIGRRAFLAG SAASAALAAT RAAAAPILSA TNFGLTLAAA QRRNGWIEVD AAAFEANIET
LRKLVAPSRI CAVMKADAYG NGIALLIPSV IRAGITDVAI TSNDEARVAR QLGYRGRLYR
IRLAHPEEME DALGLGLVEL IGNPEAAARL EAIWLKRRAR FPLPVHLALN AGGMSRNGVE
LSTDYGKADA HALLALKGLR IAGAMTHYPS EEAPDILGQL ARYKADLAWL QGEGLKADAF
TRHTANTFAT LTQPDTWLDM VRVGGALYGD PGSVKTSAFI PVPTIKSRVA AVNHYPAGQT
VAYDRTFRLE RESWLANVPI GYSDGVRRGF SHANRPEFPA ESKNHTEVLI RGRRAPIVGR
VTMNTLMVDV TEHRDVSLDD EVVLFGAQGA DRITQAEFEA NSSAYAPEML AVLGATLPRV
LKPL
//