ID C6ADS2_BARGA Unreviewed; 414 AA.
AC C6ADS2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=nifS2 {ECO:0000313|EMBL:ACS51327.1};
GN OrderedLocusNames=Bgr_10660 {ECO:0000313|EMBL:ACS51327.1};
OS Bartonella grahamii (strain as4aup).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS51327.1, ECO:0000313|Proteomes:UP000001489};
RN [1] {ECO:0000313|EMBL:ACS51327.1, ECO:0000313|Proteomes:UP000001489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT "Run-off replication of host-adaptability genes is associated with gene
RT transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL PLoS Genet. 5:E1000546-E1000546(2009).
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 -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP001562; ACS51327.1; -; Genomic_DNA.
DR RefSeq; WP_015856382.1; NC_012846.1.
DR AlphaFoldDB; C6ADS2; -.
DR STRING; 634504.Bgr_10660; -.
DR KEGG; bgr:Bgr_10660; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_5_5; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000001489; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR CDD; cd06453; SufS_like; 1.
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; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 33..401
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 414 AA; 46746 MW; A360A7593FC21FEB CRC64;
MENNVKTFTY NVEEIRRDFP LLHHQVYGKR LAYLDSSASA QKPMSVLNAM NNYYHYSYAN
VHRGMYFLAN IATQSYENSR ETVRVFLNAQ KAEEIVFTKN ATEAINTVAY GWAMPKLKEG
DEIVLTIMEH HSNIIPWHFL REQKGVKLIF VPVDENGVLH IEDFQKALSE KTRLVAITHM
SNILGTVPPV KEIIKLAHQN SIPVLVDGSQ GAVHLTVDVQ DLDCDWYVFT GHKLYGPTGI
GVLYGKEDRL EEMRPFQGGG EMIEEVTTDK VFYNAPPYRF EAGTPPIVEA IGLTAAIDYI
QEKGRSTIHA HERSLLAYAQ EKLKMVKSLR IYGHSPNKGA IISFTIEGIH AHDIAMFIDR
KGVAIRAGTH CAQPLLQRFG LTSICRASLA MYNTQEDVDQ LVEALKETRT FFNG
//
