ACLR_ACHOB
ID ACLR_ACHOB Reviewed; 436 AA.
AC Q7M181;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=2-aminohexano-6-lactam racemase;
DE EC=5.1.1.15;
DE AltName: Full=2-amino-hexano-6-lactam racemase;
DE AltName: Full=Alpha-amino-epsilon-caprolactam racemase;
OS Achromobacter obae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=37486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Naoko N., Oshihara W., Yanai A.;
RT "Alpha-amino-epsilon-caprolactam racemase for L-lysine production.";
RL (In) Korpela T., Christen P. (eds.);
RL Biochemistry of Vitamin B6, pp.449-452, Birkhauser Verlag, Basel (1987).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=3955003; DOI=10.1021/bi00350a017;
RA Ahmed S.A., Esaki N., Tanaka H., Soda K.;
RT "Mechanism of alpha-amino-epsilon-caprolactam racemase reaction.";
RL Biochemistry 25:385-388(1986).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND EPSILON-CAPROLACTAM, PYRIDOXAL PHOSPHATE AT LYS-267, ACTIVE SITE,
RP FUNCTION, AND SUBUNIT.
RX PubMed=19146406; DOI=10.1021/bi801574p;
RA Okazaki S., Suzuki A., Mizushima T., Kawano T., Komeda H., Asano Y.,
RA Yamane T.;
RT "The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I
RT racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter
RT obae.";
RL Biochemistry 48:941-950(2009).
CC -!- FUNCTION: catalyzes the interconversion of L-alpha-amino-epsilon-
CC caprolactam and D-alpha-amino-epsilon-caprolactam.
CC {ECO:0000269|PubMed:19146406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-2-aminohexano-6-lactam = D-2-aminohexano-6-lactam;
CC Xref=Rhea:RHEA:14813, ChEBI:CHEBI:58113, ChEBI:CHEBI:58609;
CC EC=5.1.1.15; Evidence={ECO:0000269|PubMed:3955003};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19146406}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR PIR; JC1497; JC1497.
DR PDB; 2ZUK; X-ray; 2.41 A; A/B=1-436.
DR PDB; 3DXV; X-ray; 2.21 A; A/B=1-436.
DR PDB; 3DXW; X-ray; 2.41 A; A/B=1-436.
DR PDBsum; 2ZUK; -.
DR PDBsum; 3DXV; -.
DR PDBsum; 3DXW; -.
DR AlphaFoldDB; Q7M181; -.
DR SMR; Q7M181; -.
DR BRENDA; 5.1.1.10; 76.
DR BRENDA; 5.1.1.15; 76.
DR EvolutionaryTrace; Q7M181; -.
DR GO; GO:0047463; F:2-aminohexano-6-lactam racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate.
FT CHAIN 1..436
FT /note="2-aminohexano-6-lactam racemase"
FT /id="PRO_0000430444"
FT ACT_SITE 137
FT /evidence="ECO:0000305|PubMed:19146406"
FT BINDING 110..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 137
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 238..241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:19146406"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 318..339
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:3DXV"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:3DXV"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:3DXV"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:3DXV"
SQ SEQUENCE 436 AA; 45699 MW; 85D1FC7936F7DDE5 CRC64;
MTKALYDRDG AAIGNLQKLR FFPLAISGGR GARLIEENGR ELIDLSGAWG AASLGYGHPA
IVAAVSAAAA NPAGATILSA SNAPAVTLAE RLLASFPGEG THKIWFGHSG SDANEAAYRA
IVKATGRSGV IAFAGAYHGC TVGSMAFSGH SVQADAAKAD GLILLPYPDP YRPYRNDPTG
DAILTLLTEK LAAVPAGSIG AAFIEPIQSD GGLIVPPDGF LRKFADICRA HGILVVCDEV
KVGLARSGRL HCFEHEGFVP DILVLGKGLG GGLPLSAVIA PAEILDCASA FAMQTLHGNP
ISAAAGLAVL ETIDRDDLPA MAERKGRLLR DGLSELAKRH PLIGDIRGRG LACGMELVCD
RQSREPARAE TAKLIYRAYQ LGLVVYYVGM NGNVLEFTPP LTITETDIHK ALDLLDRAFS
ELSAVSNEEI AQFAGW
