Q7N8L5

PR
Gene name
cysI
Protein name
Sulfite reductase [NADPH] hemoprotein beta-component
Names
SiR-HP, SiRHP
Species
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
KEGG Pathway
plu:plu0704
EC number
1.8.1.2: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-55 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q7N8L5

Entry ID Method Resolution Chain Position Source
AF-Q7N8L5-F1 Predicted AlphaFoldDB

No variants for Q7N8L5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7N8L5

No associated diseases with Q7N8L5

5 regional properties for Q7N8L5

Type Name Position InterPro Accession
domain Nitrite/Sulfite reductase ferredoxin-like domain 80 - 138 IPR005117-1
domain Nitrite/Sulfite reductase ferredoxin-like domain 353 - 412 IPR005117-2
binding_site Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site 430 - 448 IPR006066-1
binding_site Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site 478 - 496 IPR006066-2
domain Nitrite/sulphite reductase 4Fe-4S domain 173 - 331 IPR006067

Functions

Description
EC Number 1.8.1.2 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
sulfite reductase complex (NADPH) A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide.

5 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
sulfite reductase (NADPH) activity Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.

3 GO annotations of biological process

Name Definition
cysteine biosynthetic process The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid.
hydrogen sulfide biosynthetic process The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
sulfate assimilation The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNDKQHGPFI VEGKLADSER MKQESNFLRG TISEDLTNGL TGGFEGDNFL LIRFHGMYQQ
70 80 90 100 110 120
DDRDIRAERA EQKLEPRHAI MLRCRLPGGV ITPQQWLGID KFAEENTLYG SIRLTNRQTF
130 140 150 160 170 180
QFHGILKGKV KLAHQLLNQV GLDSLATAND VNRNVLCTSN PIQSELHQQA YEWAKKISEH
190 200 210 220 230 240
LLPRTRAYAE LWLDKEKVAT TDEEPILGST YLPRKFKTTV VIPPQNDVDL HANDLNFIAI
250 260 270 280 290 300
AEGSKLVGFN VLVGGGLAMT HGDKNTYPSM ASEFGYIPLE HTLAIAEAVV TTQRDWGNRT
310 320 330 340 350 360
ERKNAKTKYT LERVGVETFK AEVERRAGVK FEAIRPYEFT GRGDQIGWLK GIDDKWHLTL
370 380 390 400 410 420
FIENGRLLDY PGKPLKSGVA EIAKIHKGDF RLTANQNLII AGIPESEKQR IETIACRHGL
430 440 450 460 470 480
IDDKTTVQRK NSMACVSFPT CPLAMAEAER FLPEFVTHVE QLMNKHGIGD EHIVLRVTGC
490 500 510 520 530 540
PNGCARAMLA EVGLVGKALD RYNLHLGGNR IGTRIPRMYK ENISSQAILS IMDELIGRWA
550 560 570
TGRQPNEGFG DFLIRTDIIK PVLDSARDFY DWQEAV