ID A0A2V3DPL7_9MICC Unreviewed; 470 AA.
AC A0A2V3DPL7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=CVS29_12045 {ECO:0000313|EMBL:PXA64922.1};
OS Arthrobacter psychrochitiniphilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=291045 {ECO:0000313|EMBL:PXA64922.1, ECO:0000313|Proteomes:UP000246303};
RN [1] {ECO:0000313|EMBL:PXA64922.1, ECO:0000313|Proteomes:UP000246303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP3 {ECO:0000313|EMBL:PXA64922.1,
RC ECO:0000313|Proteomes:UP000246303};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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:PXA64922.1}.
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DR EMBL; QHLZ01000007; PXA64922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3DPL7; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000246303; Unassembled WGS sequence.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000246303}.
FT DOMAIN 38..419
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 470 AA; 49410 MW; 53D7779976354D32 CRC64;
MSSAVLDATQ LIDSPLLPVV GQDLAAPLIH GGHVRYANLD YAASAPAIKD VAAHLNEVLP
FYASVHRGAG FASQVSTSVY ENARKIVAGF VGARPDDTVI FTRNTTDSLN LLAGCVESIL
QQRGFTEGRS NVHGEVLYLD IEHHANLLPW QALPHRSVVG ADSIAATLDR VETALRAGNV
LLVAVTGASN VTGEVLPVAE LTALAHRYGA RIVLDAAQLA PHRRIDLTAT GIDYLAFSGH
KLYAPFGAGV LVGRPDWLDA GHPHLAGGGA VKDVRLESIS WTTGPARHEG GTPNVLGAAT
LAKATSVLAA LNADDWHQHE QQLRAHLVAG LNELEGVTVH SLFSDADTYP DCGSIGVVNF
SVTGYDAGLV AAYLSAEHGV GVRDGKFCAH PLLNRLGLPA GSLRASFGVG SQLEDAQRLV
AGIQTLLQEG LGWDYVVDSG RWVPVNDNRE YPSWAPNTPG TAGAAPCSIH
//
