Reviewed, UniProtKB/Swiss-Prot Q1LTP1 (CYSJ_BAUCH)

Names and origin

Protein names

Recommended name:
    Sulfite reductase [NADPH] flavoprotein alpha-component
      Short name=SIR-FP
    EC=1.8.1.2

Gene names

Name:	cysJ
Ordered Locus Names:	BCI_0218

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component By similarity.
Catalytic activity	H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01541
Cofactor	Binds 1 FAD per subunit By similarity. Binds 1 FMN per subunit By similarity.
Subunit structure	Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein By similarity.
Sequence similarities	Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Electron transport Transport
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 595	595	Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541		PRO_0000292965
Regions
	Domain	59 – 197	139	Flavodoxin-like
	Domain	230 – 444	215	FAD-binding FR-type
	Nucleotide binding	65 – 69	5	FMN By similarity
	Nucleotide binding	145 – 176	32	FMN By similarity
	Nucleotide binding	232 – 284	53	FAD By similarity
	Nucleotide binding	468 – 595	128	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LTP1-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: F6F314B06CE8CAAC	FASTA	595	67,733
	10 20 30 40 50 60 MTQQNAPKDL PPLSAEQLDR LQAISSDLSN LQLAWASGYL WNKASHSIPI DYTASQQVIT 70 80 90 100 110 120 VLSASQTGNA RRLAVQLYED LLAAQLSVVI INAGDYKFKQ IAQEKWLLIV TSTQGDGDPP 130 140 150 160 170 180 EEAIALYKYL FSKKAPVLNN IQFAIFGLGD SSYTYFAKIG KDFDSRLAEL GAQRLYDRVD 190 200 210 220 230 240 ADVDYQEKAD IWRREIVKIL QTKLVTVNAK QQLSVINNRI EVKNNLYTKE EPFTAHLVVK 250 260 270 280 290 300 QKITSRSSKK DIRHLEIDIA GSGLNYQPGD ALGVWYENDP VLISEILELL GLTGNELVQV 310 320 330 340 350 360 KEKNIPLNEA LQKHYELTNN TAEIVKSYAY ITRNSSLLAL VDDQQQLKQF AFSTPFIDMI 370 380 390 400 410 420 QRIPVELHPK QLLTLLRPLM PRLYSIASSQ AEVGDEVHLT VSVVRYEIDG KIRTGGASSY 430 440 450 460 470 480 LAYRLQESEP IRVFIEHNDN FRLPNNPNTA IIMIGSGTGI APFRGFMQQR EATTAKGKNW 490 500 510 520 530 540 LFFGNQHLTD DFLYQVEWQR YIKNGLLNKI DVAWSQDQNK KIYVQDRLLE KGIELWNWIQ 550 560 570 580 590 DGAHIYVCGN ANLMARDVEK ALVKLIAIHG RMDYEQADEF LSELRIARRF QRDTY

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF14003.1.
RefSeq	YP_588673.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4056751.
GenomeReviews	Gene locus BCI_0218 in contig CP000238_GR.
KEGG	bci:BCI_0218.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LTP1.
OMA	Q1LTP1. EQLAWVS.
Family and domain databases
HAMAP	MF_01541. [Tree]
InterPro	IPR010199. CysJ. IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
TIGRFAMs	TIGR01931. cysJ. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSJ_BAUCH

Accession

Primary (citable) accession number: Q1LTP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)