ID F4HFC8_GALAU Unreviewed; 407 AA.
AC F4HFC8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=UMN179_02198 {ECO:0000313|EMBL:AEC18211.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC18211.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC18211.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC18211.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
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}.
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DR EMBL; CP002667; AEC18211.1; -; Genomic_DNA.
DR RefSeq; WP_013746967.1; NC_015460.1.
DR AlphaFoldDB; F4HFC8; -.
DR STRING; 1005058.UMN179_02198; -.
DR KEGG; gan:UMN179_02198; -.
DR PATRIC; fig|1005058.3.peg.2185; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_3_6; -.
DR Proteomes; UP000006908; Chromosome.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 29..394
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 407 AA; 45663 MW; 27B2DF02DF4C45D8 CRC64;
MSLRAIMQSF TIEQFRHDFP FFQTENAAVY LDSAATTLRP QTLIDTTVEF YRSAGSVHRS
QYDWQQTQRF EQARQLAANF IGAENQDCIV WTSGTTHSLN AIAYGLDHFL QAGDQIIISE
AEHHANFVIW QQLALQKQLQ LTVLPLQTNY KIDENALVQA LSANTKIVAL NWVSNVTGYS
QPIEQFCTLI RQLAVNAFIV VDAAQAVLQH KMNLQTLDID FIAFSAHKLF GPTGLGVLSG
KKTALEQLRP LFYGGKMVES VTPQSSTFQP LPYRLEAGTP NIAAVIGFGA VLAWLQQYHH
ATLAHHTLTL ANLARLRLAQ YPHCRVFSAN DGHIVSFVFD NIENSDLSTL LSEQQIALRA
GQHCAQPYLH FLHQYGTLRL SFAPYNNQQD IERFFAALDN ALAILEE
//
