1A1D_PYRHO
ID 1A1D_PYRHO Reviewed; 325 AA.
AC O57809;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase;
DE Short=ACC deaminase;
DE EC=3.5.99.7;
GN OrderedLocusNames=PH0054; ORFNames=PHBE027;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000001; BAA29122.1; ALT_INIT; Genomic_DNA.
DR PIR; C71224; C71224.
DR RefSeq; WP_010884169.1; NC_000961.1.
DR PDB; 1J0A; X-ray; 2.50 A; A/B/C=1-325.
DR PDB; 1J0B; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-325.
DR PDBsum; 1J0A; -.
DR PDBsum; 1J0B; -.
DR AlphaFoldDB; O57809; -.
DR SMR; O57809; -.
DR STRING; 70601.3256439; -.
DR EnsemblBacteria; BAA29122; BAA29122; BAA29122.
DR GeneID; 1443951; -.
DR KEGG; pho:PH0054; -.
DR eggNOG; arCOG01435; Archaea.
DR OMA; LVQEKWV; -.
DR OrthoDB; 35277at2157; -.
DR BRENDA; 4.3.1.17; 5244.
DR BRENDA; 4.3.1.18; 5244.
DR EvolutionaryTrace; O57809; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..325
FT /note="Putative 1-aminocyclopropane-1-carboxylate
FT deaminase"
FT /id="PRO_0000184523"
FT MOD_RES 54
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1J0B"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1J0A"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:1J0A"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:1J0A"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:1J0A"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:1J0B"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:1J0A"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:1J0A"
SQ SEQUENCE 325 AA; 35188 MW; 60AE1B7A37CDF231 CRC64;
MHPKIFALLA KFPRVELIPW ETPIQYLPNI SREIGADVYI KRDDLTGLGI GGNKIRKLEY
LLGDALSKGA DVVITVGAVH SNHAFVTGLA AKKLGLDAIL VLRGKEELKG NYLLDKIMGI
ETRVYDAKDS FELMKYAEEI AEELKREGRK PYVIPPGGAS PIGTLGYVRA VGEIATQSEV
KFDSIVVAAG SGGTLAGLSL GLSILNEDIR PVGIAVGRFG EVMTSKLDNL IKEAAELLGV
KVEVRPELYD YSFGEYGKIT GEVAQIIRKV GTREGIILDP VYTGKAFYGL VDLARKGELG
EKILFIHTGG ISGTFHYGDK LLSLL
