Q9T467

PR
Gene name
chlB
Protein name
Light-independent protochlorophyllide reductase subunit B
Names
DPOR subunit B, LI-POR subunit B
Species
Nephroselmis olivacea (Green alga)
KEGG Pathway
EC number
1.3.7.7: With an iron-sulfur protein as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

123-194 (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 Q9T467

Entry ID Method Resolution Chain Position Source
AF-Q9T467-F1 Predicted AlphaFoldDB

No variants for Q9T467

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9T467

No associated diseases with Q9T467

2 regional properties for Q9T467

Type Name Position InterPro Accession
domain Nitrogenase/oxidoreductase, component 1 12 - 428 IPR000510
domain Light-independent protochlorophyllide reductase subunit B-like, C-terminal 465 - 509 IPR013580

Functions

Description
EC Number 1.3.7.7 With an iron-sulfur protein as acceptor
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.

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.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on iron-sulfur proteins as donors Catalysis of an oxidation-reduction (redox) reaction in which an iron-sulfur protein acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces an iron-sulfur protein.

2 GO annotations of biological process

Name Definition
light-independent chlorophyll biosynthetic process The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
photosynthesis, dark reaction A complex cycle of enzyme-mediated reactions which catalyzes the reduction of carbon dioxide to sugar. As well as carbon dioxide the cycle requires reducing power in the form of reduced nicotinamide adenine dinucleotide phosphate (NADP) and chemical energy in the form of adenosine triphosphate (ATP). The reduced NADP (NADPH) and ATP are produced by the 'light' reactions.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLAYWMYAG PAHLGVLRVA SSFKNVHAIM HAPLGDDYFN VMSSMLERDR DFTPVTASIV
70 80 90 100 110 120
DRHVLATGSQ RKVVATIHRK DQEDEPDLIL VTPTCTSSIL QEDLGNYVAR AAPYTKSEVL
130 140 150 160 170 180
LADVQHYRIH ELQAQDRILE QVVRHIMDPE RQKGTLDTTP TPTPSANLIG FFDLGFHHRD
190 200 210 220 230 240
DSRELRRLLH GLGIEINSVL PKGGSIPDLH QLAKAWFNII PYREAGLMTA KYLEESFHIP
250 260 270 280 290 300
YIDRTPIGLI ETRKFIGEIE AILQTRGVDR HEYYEKFIIH HETIVSQAAW FARSIDCQNL
310 320 330 340 350 360
LGKRVIVFGD CTHAATITKL LVRELGIHVV CAGTYCKYDE AWFREQVNGY VDEILITEDH
370 380 390 400 410 420
TQVADTISRL EPAAIFGTQM ERHVGKRLDI PCGVISAPAH IQNFPLSFRP FLGYEGTNVV
430 440 450 460 470 480
ADLIYNTFRL GMEDHLLELF GGHDTKQIGE SQMAESISNS KGCQWTPEAE KELAHIPRFV
490 500 510 520 530
RSKVKRATER FAQEHGYPVI NLECIYLAKQ STSVDIETIQ HLLFNDETEV Q